Powdered pouch and method of making same

ABSTRACT

Disclosed herein are water-soluble films and resulting packets including a water-soluble film coated by a powder, wherein the powder includes a mixture of a powdered lubricant and an active agent. Optionally, the active agent may be encapsulated, e.g. microencapsulated, for release of the active agent through mechanisms including, but not limited to, mechanical rupture, melt, ablation, dissolution, diffusion, biodegradation, or pH-controlled release. Active ingredients described include enzymes, oils, flavors, colorants, odor absorbers, fragrances, pesticides, fertilizers, activators, acid catalysts, metal catalysts, ion scavengers, bleaches, bleach components, fabric softeners and combinations thereof. Examples of packet fills include laundry detergents, bleach and laundry additives, fabric care, dishwashing, hard surface cleaning, beauty care, skin care, other personal care, and foodstuffs.

CROSS REFERENCE TO RELATED APPLICATION

This is a continuation of U.S. patent application Ser. No. 13/828,299,filed Mar. 14, 2013, which claims the benefit under 35 U.S.C. § 119(e)of U.S. Provisional Patent Application No. 61/624,926, filed Apr. 16,2012. The entire disclosures of the foregoing applications areincorporated herein by reference.

FIELD OF THE INVENTION

The present disclosure relates generally to water-soluble films andrelated packets. More particularly the disclosure relates to watersoluble films and packets comprised of water-soluble films coated by apowder that includes an active agent.

BACKGROUND

Water-soluble packets are known in the art. These compositions have theadvantage that they are easy to dose, handle, transport and store.

The film material used in water-soluble packets is often relativelyfragile since in most applications it must release the product quicklyand completely in water, and without leaving residue. To achieve this,the film material must be thin and must have a high water-reactivity.

The incorporation of powder into film material is known in the art. Apolyvinyl alcohol-type film can be obtained by distributing an aqueousdispersion of a fine powder on one or both sides and then drying thefilm, for example for good slip properties and adhesion resistance.

In addition, powdering of film material is known. A dusting treatmentagent for imparting inter-film lubricity to a film of thermoplasticresin has been described. In packets containing liquid compositions,powdering has been used to reduce the negative effects of weeping, suchas a tacky feel or premature loss of product. Additionally, thewater-soluble nature of such packets often renders them vulnerable tohumidity, which can weaken the structural integrity of the film.Exposure to humid conditions often results in the packets stickingtogether and packet failure upon separation.

SUMMARY

One aspect of the disclosure is a water-soluble packet comprising awater-soluble film in the form of a packet and coated by a powder,wherein the powder comprises a mixture of a powdered lubricant and anactive agent, wherein the active agent is not a fragrance. Optionally,the active agent may be encapsulated.

Another aspect of the disclosure is a water-soluble packet comprising awater-soluble film in the form of a packet and coated by a powder,wherein the powder comprises a mixture of a powdered lubricant and anactive agent which comprises a microencapsulated fragrance.

Still another aspect of the disclosure is a method of providing awater-soluble film and/or film packet additional functionality,including the steps of coating a water-soluble film and/or film packetwith a powder comprising an active agent. The water soluble packet andpowder are made according to the disclosure herein. Optionally, theactive agent can be encapsulated.

While the disclosure of preferred embodiments herein providesdescriptions of film packets, the powdered film itself, prior toformation into a packet is also contemplated, such that for anyembodiment describing a packet, a film is equally contemplated. Thus,another aspect of the disclosure is a water-soluble film coated by apowder, wherein the powder comprises a mixture of a powdered lubricantand an active agent, wherein the active agent is not a fragrance.Optionally, the active agent may be encapsulated. Another aspect of thedisclosure is a water-soluble film coated by a powder, wherein thepowder comprises a mixture of a powdered lubricant and an active agentwhich comprises a microencapsulated fragrance.

Further aspects and advantages will be apparent to those of ordinaryskill in the art from a review of the following detailed description.While the compositions and methods are susceptible of embodiments invarious forms, the description hereafter includes specific embodimentswith the understanding that the disclosure is illustrative, and is notintended to limit the invention to the specific embodiments describedherein.

BRIEF DESCRIPTION OF THE DRAWINGS

FIG. 1 shows an interval plot of the numerical value (and 95% confidenceinterval) of the odor perceived from each pouch type tested according tothe Example described below.

DETAILED DESCRIPTION

Disclosed herein are water-soluble films and packets comprising awater-soluble film in the form of a packet and coated by a powder,wherein the powder comprises a mixture of a powdered lubricant and anactive agent. Optionally, the active agent is microencapsulated. In onetype of embodiment, the active agent comprises a microencapsulatedfragrance. In embodiments, the microcapsule provides for a controlledrelease of the active agent through mechanisms including, but notlimited to, mechanical rupture, melt, ablation, dissolution, diffusion,biodegradation, or pH-controlled release.

One type of embodiment of the water-soluble packets will comprise,enclosed within the packet, solid, liquid or gel compositions, orcombinations thereof. Non-limiting examples of the enclosed compositioninclude laundry detergents, bleach and laundry additives, fabric care,dishwashing, hard surface cleaning, beauty care, skin care, otherpersonal care, or food product compositions.

The disclosure further provides a method of providing additionalfunctionality to a water-soluble packet through the powder coating. Thepowder coating is comprised of a powder lubricant and an active agent.This combination has been demonstrated to be particularly advantageousin providing the packet with additional functionality while improvingthe feel of the packet surface, mitigating potential weeping of liquidproducts onto surface of the packet, and preventing the packets fromsticking together, thereby preventing possible failure duringseparation. The water-soluble packets of the disclosure herein can haveone or more other, optional advantages including, delivering an activeagent to a substrate before the water-soluble packet is dissolved,providing a controlled and delayed release of the active agent,providing an accurate dosing of active agent and enabling the packet tocomprise more than one active agent per packet. In particular,water-soluble packets according to one class of embodiments of thedisclosure can demonstrate advantageous stability if one or more of theactive agents is known to be unstable in the presence of another activeagent or in the presence of a component of the composition enclosedwithin the packet. Additionally, the method of providing the packetadditional functionality through the incorporation of the active agentinto the powder coating is advantageous because no new processingequipment is needed to produce the packet.

Ranges may be expressed herein as from “about” or “approximately” oneparticular value and/or to “about” or “approximately” another particularvalue. When such a range is expressed, another contemplated embodimentincludes from the one particular value and/or to the other particularvalue. Similarly, when particular values are expressed asapproximations, but use antecedents such as “about,” “at least,” or“less than about,” it will be understood that the particular value formsanother embodiment.

As used herein, the term “comprising” indicates the potential inclusionof other agents, elements, steps, or features, in addition to thosespecified.

As used herein and unless specified otherwise all measurements ofviscosity in centipoises (cP) are of a 4% solution at 20° C.

As used herein and unless specified otherwise, the terms “wt. %” and “wt%” are intended to refer to the composition of the identified element in“dry” (non water) parts by weight of the entire film (when applicable)or parts by weight of the entire composition enclosed within a packet(when applicable). As used herein and unless specified otherwise, theterm “phr” is intended to refer to the composition of the identifiedelement in parts per one hundred parts water-soluble polymer resin.

As used herein, the term “coating powder” refers to the mixture ofpowdered lubricant and active agent. Optionally the active agent may bemicroencapsulated.

The packet includes a water-soluble film as at least one wall of thepacket, and optionally the water-soluble film is the sole film componentof the packet. Water-soluble films of this type which can be made intopackets, optional ingredients for use therein, and methods of making thesame are well known in the art.

In one class of embodiments, the water-soluble film includes PVOH. PVOHis a synthetic resin generally prepared by the alcoholysis, usuallytermed hydrolysis or saponification, of polyvinyl acetate. Fullyhydrolyzed PVOH, wherein virtually all the acetate groups have beenconverted to alcohol groups, is a strongly hydrogen-bonded, highlycrystalline polymer which dissolves only in hot water—greater than about140° F. (60° C.). If a sufficient number of acetate groups are allowedto remain after the hydrolysis of polyvinyl acetate, the PVOH polymerthen being known as partially hydrolyzed, it is more weaklyhydrogen-bonded and less crystalline and is soluble in cold water—lessthan about 50° F. (10° C.). An intermediate cold/hot water soluble filmcan include, for example, intermediate partially-hydrolyzed PVOH (e.g.,with degrees of hydrolysis of about 94% to about 98%), and is readilysoluble only in warm water—e.g., rapid dissolution at temperatures ofabout 40° C. and greater. Both fully and partially hydrolyzed PVOH typesare commonly referred to as PVOH homopolymers although the partiallyhydrolyzed type is technically a vinyl alcohol-vinyl acetate copolymer.

The degree of hydrolysis of the PVOH included in the water-soluble filmsof the present disclosure can be about 75% to about 99%, for example. Asthe degree of hydrolysis is reduced, a film made from the resin willhave reduced mechanical strength but faster solubility at temperaturesbelow about 20° C. As the degree of hydrolysis increases, a film madefrom the resin will tend to be mechanically stronger and thethermoformability will tend to decrease. The degree of hydrolysis of thePVOH can be chosen such that the water-solubility of the resin istemperature dependent, and thus the solubility of a film made from theresin, and additional ingredients is also influenced. In one class ofembodiments the film is cold water-soluble. A cold water-soluble film,soluble in water at a temperature of less than 10° C., can include PVOHwith a degree of hydrolysis in a range of about 75% to about 90%, or ina range of about 80% to about 90%, or in a range of about 85% to about90%. In another class of embodiments the film is hot water-soluble. Ahot water-soluble film, soluble in water at a temperature of at leastabout 60° C., can include PVOH with a degree of hydrolysis of at leastabout 98%.

Other film-forming resins for use in addition to or in an alternative toPVOH can include, but are not limited to, modified polyvinyl alcohols,polyacrylates, water-soluble acrylate copolymers, polyaminopropylsulfonic acid and salts thereof, polyitaconic acid and salts thereof,polyacryamides, polyvinyl pyrrolidone, pullulan, cellulosics, includingbut not limited to carboxymethyl cellulose and hydroxypropyl methylcellulose, water-soluble natural polymers including, but not limited to,guar gum, xanthan gum, carrageenan, and starch, water-soluble polymerderivatives including, but not limited to, modified starches, includingethoxylated starch and hydroxypropylated starch, poly(sodiumacrylamido-2-methylpropane sulfonate), polymonomethylmaleate and saltsthereof, copolymers thereof, and combinations of any of the foregoingwith each other and/or with PVOH.

The water-soluble resin can be included in the water-soluble film in anysuitable amount, for example an amount in a range of about 35 wt % toabout 90 wt %. The weight ratio of the amount of the water-soluble resinas compared to the combined amount of additives can be any suitableratio, for example a ratio in a range of about 0.5 to about 5, or about1 to 3, or about 1 to 2.

Water-soluble resins for use in the films described herein (including,but not limited to PVOH resins) can be characterized by any suitableviscosity for the desired film properties, optionally a viscosity in arange of about 8.0 to about 40.0 cP, or about 10.0 cP to about 30 cP, orabout 13 cP to about 27 cP. The viscosity of a PVOH resin is determinedby measuring a freshly made solution using a Brookfield LV typeviscometer with UL adapter as described in British Standard EN ISO15023-2:2006 Annex E Brookfield Test method. It is internationalpractice to state the viscosity of 4% aqueous solution at 20° C. Allviscosities specified herein in cP should be understood to refer to theviscosity of 4% aqueous solution at 20° C., unless specified otherwise.

It is well known in the art that the viscosity of a resin is correlatedwith the weight average molecular weight (Mw) of the same resin, andoften the viscosity is used as a proxy for Mw. Thus, the weight averagemolecular weight of the water-soluble resin optionally can be in a rangeof about 35,000 to about 205,000, or about 80,000 to about 170,000, orabout 97,000 to about 160,000 Daltons. The molecular weight of the resinneed only be sufficient to enable it to be molded by suitable techniquesto form a thin plastic film.

The water-soluble films according to the present disclosure may includeother optional additive ingredients including, but not limited to,plasticizers, surfactants, emulsifiers, fillers, extenders, antiblockingagents, detackifying agents, antifoams, film formers and otherfunctional ingredients, for example in amounts suitable for theirintended purpose.

Water is recognized as a very efficient plasticizer for PVOH and otherpolymers; however, the volatility of water makes its utility limitedsince polymer films need to have at least some resistance (robustness)to a variety of ambient conditions including low and high relativehumidity. Glycerin is much less volatile than water and has been wellestablished as an effective plasticizer for PVOH and other polymers.Glycerin or other such liquid plasticizers by themselves can causesurface “sweating” and greasiness if the level used in the filmformulation is too high. This can lead to problems in a film such asunacceptable feel to the hand of the consumer and even blocking of thefilm on the roll or in stacks of sheets if the sweating is not mitigatedin some manner, such as powdering of the surface. This could becharacterized as over plasticization. However, if too little plasticizeris added to the film the film may lack sufficient ductility andflexibility for many end uses, for example to be converted into a finaluse format such as packets.

Plasticizers for use in water-soluble films of the present disclosureinclude, but are not limited to, sorbitol, glycerol, diglycerol,propylene glycol, ethylene glycol, diethyleneglycol, triethylene glycol,tetraethyleneglycol, polyethylene glycols up to MW 400, 2 methyl 1, 3propane diol, lactic acid, monoacetin, triacetin, triethyl citrate,1,3-butanediol, trimethylolpropane (TMP), polyether triol, andcombinations thereof. As less plasticizer is used, the film can becomemore brittle, whereas as more plasticizer is used the film can losetensile strength. Plasticizers can be included in the water-solublefilms in an amount in a range of about 25 phr to about 50 phr, or fromabout 30 phr to about 45 phr, or from about 32 phr to about 42 phr, forexample.

Surfactants for use in water-soluble films are well known in the art.Optionally, surfactants are included to aid in the dispersion of theresin solution upon casting. Suitable surfactants for water-solublefilms of the present disclosure include, but are not limited to, dialkylsulfosuccinates, lactylated fatty acid esters of glycerol and propyleneglycol, lactylic esters of fatty acids, sodium alkyl sulfates,polysorbate 20, polysorbate 60, polysorbate 65, polysorbate 80, alkylpolyethylene glycol ethers, lecithin, acetylated fatty acid esters ofglycerol and propylene glycol, sodium lauryl sulfate, acetylated estersof fatty acids, myristyl dimethylamine oxide, trimethyl tallow alkylammonium chloride, quaternary ammonium compounds, salts thereof andcombinations of any of the forgoing. Too little surfactant can sometimesresult in a film having holes, whereas too much surfactant can result inthe film having a greasy or oily feel from excess surfactant present onthe surface of the film. Thus, surfactants can be included in thewater-soluble films in an amount of less than about 2 phr, for exampleless than about 1 phr, or less than about 0.5 phr, for example.

One type of secondary component contemplated for use is a defoamer.Defoamers can aid in coalescing of foam bubbles. Suitable defoamers foruse in water-soluble films according to the present disclosure include,but are not limited to, hydrophobic silicas, for example silicon dioxideor fumed silica in fine particle sizes, including Foam Blast® defoamersavailable from Emerald Performance Materials, including Foam Blast® 327,Foam Blast® UVD, Foam Blast® 163, Foam Blast® 269, Foam Blast® 338, FoamBlast® 290, Foam Blast® 332, Foam Blast® 349, Foam Blast® 550 and FoamBlast® 339, which are proprietary, non-mineral oil defoamers. Inembodiments, defoamers can be used in an amount of 0.5 phr, or less, forexample, 0.05 phr, 0.04 phr, 0.03 phr, 0.02 phr, or 0.01 phr.

Processes for making water-soluble articles, including films andpackets, include casting, blow-molding, extrusion and blown extrusion,as known in the art. One contemplated class of embodiments ischaracterized by the water-soluble film described herein being formed bycasting, for example, by admixing the ingredients described herein withwater to create an aqueous mixture, for example a solution withoptionally dispersed solids, applying the mixture to a surface, anddrying off water to create a film. Similarly, other compositions can beformed by drying the mixture while it is confined in a desired shape.

The film is useful for creating a packet to contain a composition, forexample laundry or dishwashing compositions, thereby forming a packet.The film described herein can also be used to make a packet with two ormore compartments made of the same film or in combination with films ofother polymeric materials. Additional films can, for example, beobtained by casting, blow-molding, extrusion or blown extrusion of thesame or a different polymeric material, as known in the art. In one typeof embodiment, the polymers, copolymers or derivatives thereof suitablefor use as the additional film are selected from polyvinyl alcohols,polyvinyl pyrrolidone, polyalkylene oxides, polyacrylic acid, cellulose,cellulose ethers, cellulose esters, cellulose amides, polyvinylacetates, polycarboxylic acids and salts, polyaminoacids or peptides,polyamides, polyacrylamide, copolymers of maleic/acrylic acids,polysaccharides including starch and gelatin, natural gums including,but not limited to, xanthan, and carrageenans. For example, polymers canbe selected from polyacrylates and water-soluble acrylate copolymers,methylcellulose, carboxymethylcellulose sodium, dextrin, ethylcellulose,hydroxyethyl cellulose, hydroxypropyl methylcellulose, maltodextrin,polymethacrylates, and combinations thereof, or selected from polyvinylalcohols, polyvinyl alcohol copolymers and hydroxypropyl methylcellulose (HPMC), and combinations thereof.

The packets of the present disclosure comprise at least one sealedcompartment. Thus the packets may comprise a single compartment ormultiple compartments. In embodiments comprising multiple compartments,each compartment may contain identical and/or different compositions. Inturn, the compositions may take any suitable form including, but notlimited to liquid, solid and combinations thereof (e.g. a solidsuspended in a liquid). In some embodiments, the packets comprises afirst, second and third compartment, each of which respectively containsa different first, second and third composition. In some embodiments,the compositions may be visually distinct as described in EuropeanPatent Application Number 09161692.0 (filed Jun. 2, 2009 and assigned tothe Procter & Gamble Company).

The compartments of multi-compartment packets may be of the same ordifferent size(s) and/or volume(s). The compartments of the presentmulti-compartment packets can be separate or conjoined in any suitablemanner. In some embodiments, the second and/or third and/or subsequentcompartments are superimposed on the first compartment. In oneembodiment, the third compartment may be superimposed on the secondcompartment, which is in turn superimposed on the first compartment in asandwich configuration. Alternatively the second and third compartmentsmay be superimposed on the first compartment. However it is also equallyenvisaged that the first, second and optionally third and subsequentcompartments may be attached to one another in a side by siderelationship. The compartments may be packed in a string, eachcompartment being individually separable by a perforation line. Henceeach compartment may be individually torn-off from the remainder of thestring by the end-user,

In some embodiments, multi-compartment packets include threecompartments consisting of a large first compartment and two smallercompartments. The second and third smaller compartments are superimposedon the first larger compartment. The size and geometry of thecompartments are chosen such that this arrangement is achievable. Thegeometry of the compartments may be the same or different. In someembodiments the second and optionally third compartment each has adifferent geometry and shape as compared to the first compartment. Inthese embodiments, the second and optionally third compartments arearranged in a design on the first compartment. The design may bedecorative, educative, or illustrative, for example to illustrate aconcept or instruction, and/or used to indicate origin of the product.In some embodiments, the first compartment is the largest compartmenthaving two large faces sealed around the perimeter, and the secondcompartment is smaller covering less than about 75%, or less than about50% of the surface area of one face of the first compartment. Inembodiments in which there is a third compartment, the aforementionedstructure may be the same but the second and third compartments coverless than about 60%, or less than about 50%, or less than about 45% ofthe surface area of one face of the first compartment.

The packets of the present disclosure may comprise one or more differentfilms. For example, in single compartment embodiments, the packet may bemade from one wall that is folded onto itself and sealed at the edges,or alternatively, two walls that are sealed together at the edges. Inmultiple compartment embodiments, the packet may be made from one ormore films such that any given packet compartment may comprise wallsmade from a single film or multiple films having differing compositions.In one embodiment, a multi-compartment packet comprises at least threewalls: an outer upper wall; an outer lower wall; and a partitioningwall. The outer upper wall and the outer lower wall are generallyopposing and form the exterior of the packet. The partitioning wall isinterior to the packet and is secured to the generally opposing outerwalls along a seal line. The partitioning wall separates the interior ofthe multi-compartment packet into at least a first compartment and asecond compartment. In one class of embodiments, the partitioning wallmay be the only enzyme containing film thereby minimizing the exposureof the consumer to the enzymes.

Packets may be made using any suitable equipment and method. Forexample, single compartment packets may be made using vertical formfilling, horizontal form filling, or rotary drum filling techniquescommonly known in the art. Such processes may be either continuous orintermittent. The film may be dampened, and/or heated to increase themalleability thereof. The method may also involve the use of a vacuum todraw the film into a suitable mold. The vacuum drawing the film into themold can be applied for about 0.2 to about 5 seconds, or about 0.3 toabout 3, or about 0.5 to about 1.5 seconds, once the film is on thehorizontal portion of the surface. This vacuum can be such that itprovides an under-pressure in a range of 10 mbar to 1000 mbar, or in arange of 100 mbar to 600 mbar, for example.

The molds, in which packets may be made, can have any shape, length,width and depth, depending on the required dimensions of the packets.The molds may also vary in size and shape from one to another, ifdesirable. For example, the volume of the final packets may be about 5ml to about 300 ml, or about 10 to 150 ml, or about 20 to about 100 ml,and that the mold sizes are adjusted accordingly.

In one embodiment, the packet includes a first and a second sealedcompartment. The second compartment is in a generally superposedrelationship with the first sealed compartment such that the secondsealed compartment and the first sealed compartment share a partitioningwall interior to the packet.

In one embodiment, the packet including a first and a second compartmentfurther includes a third sealed compartment. The third sealedcompartment is in a generally superposed relationship with the firstsealed compartment such that the third sealed compartment and the firstsealed compartment share a partitioning wall interior to the packet.

In various embodiments, the first composition and the second compositionare selected from one of the following combinations: liquid, liquid;liquid, powder; powder, powder; and powder, liquid.

In various embodiments, the first, second and third compositions areselected from one of the following combinations: solid, liquid, liquidand liquid, liquid, liquid.

In one embodiment, the single compartment or plurality of sealedcompartments contains a composition. The plurality of compartments mayeach contain the same or a different composition. The composition isselected from a liquid, solid or combination thereof.

Heat can be applied to the film in the process commonly known asthermoforming. The heat may be applied using any suitable means. Forexample, the film may be heated directly by passing it under a heatingelement or through hot air, prior to feeding it onto a surface or onceon a surface. Alternatively, it may be heated indirectly, for example byheating the surface or applying a hot item onto the film. The film canbe heated using an infrared light. The film may be heated to atemperature of at least 50° C., for example about 50 to about 150° C.,about 50 to about 120° C., about 60 to about 130° C., about 70 to about120° C., or about 60 to about 90° C.

Alternatively, the film can be wetted by any suitable means, for exampledirectly by spraying a wetting agent (including water, a solution of thefilm composition, a plasticizer for the film composition, or anycombination of the foregoing) onto the film, prior to feeding it ontothe surface or once on the surface, or indirectly by wetting the surfaceor by applying a wet item onto the film.

Once a film has been heated and/or wetted, it may be drawn into anappropriate mold, preferably using a vacuum. The film can bethermoformed with a draw ratio of at least about 1.5, for example, andoptionally up to a draw ratio of 2, for example. The filling of themolded film can be accomplished by utilizing any suitable means. In someembodiments, the most preferred method will depend on the product formand required speed of filling. In some embodiments, the molded film isfilled by in-line filling techniques. The filled, open packets are thenclosed forming the packets, using a second film, by any suitable method.This may be accomplished while in horizontal position and in continuous,constant motion. The closing may be accomplished by continuously feedinga second film, for example, a water-soluble film, over and onto the openpackets and then sealing the first and second film together, typicallyin the area between the molds and thus between the packets.

Any suitable method of sealing the packet and/or the individualcompartments thereof may be utilized. Non-limiting examples of suchmeans include heat sealing, solvent welding, solvent or wet sealing, andcombinations thereof. The water-soluble packet and/or the individualcompartments thereof can be heat sealed at a temperature of at least200° F. (93° C.), for example in a range of about 220° F. (about 105°C.) to about 290° F. (about 145° C.), or about 230° F. (about 110° C.)to about 280° F. (about 140° C.). Typically, only the area which is toform the seal is treated with heat or solvent. The heat or solvent canbe applied by any method, typically on the closing material, andtypically only on the areas which are to form the seal. If solvent orwet sealing or welding is used, heat may optionally also be applied.Suitable wet or solvent sealing/welding methods include selectivelyapplying solvent onto the area between the molds, or on the closingmaterial, by for example, spraying or printing this onto these areas,and then applying pressure onto these areas, to form the seal. Sealingrolls and belts as described above (optionally also providing heat) canbe used, for example.

The formed packets may then be cut by a cutting device. Cutting can beaccomplished using any known method. It may be preferred that thecutting is also done in continuous manner, and preferably with constantspeed and preferably while in horizontal position. The cutting devicecan, for example, be a sharp item, or a hot item, or a laser, whereby inthe latter cases, the hot item or laser ‘burns’ through the film/sealingarea.

The different compartments of a multi-compartment packets may be madetogether in a side-by-side style wherein the resulting, cojoined packetsmay or may not be separated by cutting. Alternatively, the compartmentscan be made separately.

In some embodiments, packets may be made according to a processincluding the steps of:

-   -   a) forming a first compartment (as described above);    -   b) forming a recess within some or all of the closed compartment        formed in step (a), to generate a second molded compartment        superposed above the first compartment;    -   c) filling and closing the second compartments by means of a        third film;    -   d) sealing the first, second and third films; and    -   e) cutting the films to produce a multi-compartment packet.

The recess formed in step (b) may be achieved by applying a vacuum tothe compartment prepared in step (a).

In some embodiments, second, and/or third compartment(s) can be made ina separate step and then combined with the first compartment asdescribed in European Patent Application Number 08101442.5 or WO2009/152031 (filed Jun. 13, 2008 and assigned to the Procter & GambleCompany).

In other embodiments, packets may be made according to a processincluding the steps of:

-   -   a) forming a first compartment, optionally using heat and/or        vacuum, using a first film on a first forming machine;    -   b) filling the first compartment with a first composition;    -   c) on a second forming machine, deforming a second film,        optionally using heat and vacuum, to make a second and        optionally third molded compartment;    -   d) filling the second and optionally third compartments;    -   e) sealing the second and optionally third compartment using a        third film;    -   f) placing the sealed second and optionally third compartments        onto the first compartment;    -   g) sealing the first, second and optionally third compartments;        and    -   h) cutting the films to produce a multi-compartment packet.

The first and second forming machines may be selected based on theirsuitability to perform the above process. In some embodiments, the firstforming machine can be a horizontal forming machine, and the secondforming machine can be a rotary drum forming machine, optionally locatedabove the first forming machine.

It should be understood that by the use of appropriate feed stations, itmay be possible to manufacture multi-compartment packets incorporating anumber of different or distinctive compositions and/or different ordistinctive liquid, gel or paste compositions.

The water-soluble film and/or packet described herein must be at leastpartially coated with a powder composition. The powder can be present onthe packet in an amount of at least about 0.01 mg/cm², or in a range ofabout 0.01 mg/cm² to about 10 mg/cm², for example. The outer surface ofthe film packet can be coated. In some embodiments, the inner surface ofthe film packet can be coated, in the alternative to or in addition tothe outer film surface. In one embodiment, the powder composition isapplied to the film after forming a packet. In another embodiment, thepowder composition is applied to the film before forming a packet.

The powdered lubricant is a powder that when present as the only powdercomponent aids in preventing the packets from sticking together duringconditions which can be present during film conversion, or when packetsare in close proximity, such as in secondary packaging, preventingpossible failure during separation, optionally one or more of thefollowing: temperature about 10° C. to about 40° C., or about 15° C. toabout 35° C., or about 20° C. to about 25° C.; relative humidity fromabout 10% to about 50%, or about 15% to about 45%, or about 20% to about40%, or +/−5% relative humidity of the equilibrium percent relativehumidity (eRH) of the film as received in its package. Additionally, inone class of embodiments the powdered lubricant can mitigate potentialweeping of liquid contents and thereby improve the feel of the packetsurface. When present in the coating powder composition in an amount ofat least about 1 wt %, for example, the powdered lubricant additionallyacts as a carrier for active agent and aids in uniformly dispersing theactive agent. In some embodiments, the powdered lubricant aids in themechanical rupture of the microcapsules that contain active agents.

In one type of embodiment, the powdered lubricant has an averageparticle size of at least about 0.1 μm, or in a range of about 0.1 μm toabout 100 μm, for example. Typically, a powder such as starch could beused, such a powder being well known. Other suitable materials includemodified starches (including, but not limited to, corn starch, potatostarch, or hydroxyl ethyl starch), silicas, siloxanes, calciumcarbonate, magnesium carbonate, clay, talc, silicic acid, kaolin,gypsum, zeolites, cylclodextrins, calcium stearate, zinc stearate,alumina, magnesium stearate, alumina, zinc oxide and combinations of anyof the foregoing. Generally, the powder will be inert. The powderlubricant is present in the coating powder in an amount of at leastabout 1 wt %, or in a range of about 1 wt % to about 99 wt %.

The active agent, when present in the coating powder composition in anamount of at least about 1 wt %, or in a range of about 1 wt % to about99 wt %, provides additional functionality to the packet. Inembodiments, the active agent can comprise one or more componentsincluding, but not limited to, enzymes, oils, flavors, colorants, odorabsorbers, fragrances, pesticides, fertilizers, activators, acidcatalysts, metal catalysts, ion scavengers, bleaches, bleach components,fabric softeners or combinations thereof. The active agent can take anydesired form, including as a solid, a liquid, a mull, a paste, a gas,etc., and optionally can be encapsulated.

In certain embodiments, the active agent may comprise an enzyme.Suitable enzymes include enzymes categorized in any one of the sixconventional Enzyme Commission (EC) categories, i.e., theoxidoreductases of EC 1 (which catalyze oxidation/reduction reactions),the transferases of EC 2 (which transfer a functional group, e.g., amethyl or phosphate group), the hydrolases of EC 3 (which catalyze thehydrolysis of various bonds), the lyases of EC 4 (which cleave variousbonds by means other than hydrolysis and oxidation), the isomerases ofEC 5 (which catalyze isomerization changes within a molecule) and theligases of EC 6 (which join two molecules with covalent bonds). Examplesof such enzymes include dehydrogenases and oxidases in EC 1,transaminases and kinases in EC 2, lipases, cellulases, amylases,mannanases, and peptidases (a.k.a. proteases or proteolytic enzymes) inEC 3, decarboxylases in EC 4, isomerases and mutases in EC 5 andsynthetases and synthases of EC 6.

Oxidoreductases

Oxidoreductases include, but are not limited to: those acting on theCH-OH group of donors; those acting on the aldehyde or oxo group ofdonors; those acting on the CH—CH group of donors; those acting on theCH—NH₂ group of donors; those acting on the CH—NH group of donors; thoseacting on NADH or NADPH; those acting on other nitrogenous compounds asdonors; those acting on a sulfur group of donors; those acting on a hemegroup of donors; those acting on diphenols and related substances asdonors; those acting on a peroxide as acceptor; those acting on hydrogenas donor; those acting on single donors with incorporation of molecularoxygen (oxygenases); those acting on paired donors, with incorporationor reduction of molecular oxygen; those acting on superoxide radicals asacceptor; those oxidizing metal ions; those acting on CH or CH₂ groups;those acting on iron-sulfur proteins as donors; those acting on reducedflavodoxin as donor; those acting on phosphorus or arsenic in donors;those acting on X—H and Y—H to form an X-Y bond; and those acting onhalogen in donors.

The oxidoreductases which act on the CH—OH group of donors can include,but are not limited to, those with NAD+ or NADP+ as acceptor (includingalcohol dehydrogenase, alcohol dehydrogenase (NADP⁺), homoserinedehydrogenase, (R,R)-butanediol dehydrogenase, glycerol dehydrogenase,propanediol-phosphate dehydrogenase, glycerol-3-phosphate dehydrogenase(NAD⁺), D-xylulose reductase, L-xylulose reductase, D-arabinitol4-dehydrogenase, L-arabinitol 4-dehydrogenase, L-arabinitol2-dehydrogenase, L-iditol 2-dehydrogenase, D-iditol 2-dehydrogenase,galactitol 2-dehydrogenase, mannitol-l-phosphate 5-dehydrogenase,inositol 2-dehydrogenase, glucuronate reductase, glucuronolactonereductase, aldehyde reductase, UDP-glucose 6-dehydrogenase, histidinoldehydrogenase, quinate dehydrogenase, shikimate dehydrogenase,glyoxylate reductase, L-lactate dehydrogenase, D-lactate dehydrogenase,glycerate dehydrogenase, 3-hydroxybutyrate dehydrogenase,3-hydroxyisobutyrate dehydrogenase, mevaldate reductase, mevaldatereductase (NADPH), hydroxymethylglutaryl-CoA reductase (NADPH),3-hydroxyacyl-CoA dehydrogenase, acetoacetyl-CoA reductase, malatedehydrogenase, malate dehydrogenase (oxaloacetate-decarboxylating),malate dehydrogenase (decarboxylating), malate dehydrogenase(oxaloacetate-decarboxylating) (NADP⁺), isocitrate dehydrogenase (NAD⁺),isocitrate dehydrogenase (NADP⁺), phosphogluconate 2-dehydrogenase,phosphogluconate dehydrogenase (decarboxylating), L-gulonate3-dehydrogenase, L-arabinose 1-dehydrogenase, glucose 1-dehydrogenase,galactose 1-dehydrogenase, glucose-6-phosphate dehydrogenase,3α-hydroxysteroid dehydrogenase (B-specific), 3(or 17)(β-hydroxysteroiddehydrogenase, 3α-hydroxycholanate dehydrogenase, 3α(or20(β)-hydroxysteroid dehydrogenase, allyl-alcohol dehydrogenase,lactaldehyde reductase (NADPH), ribitol 2-dehydrogenase, fructuronatereductase, tagaturonate reductase, 3-hydroxypropionate dehydrogenase,2-hydroxy-3-oxopropionate reductase, 4-hydroxybutyrate dehydrogenase,estradiol 17β-dehydrogenase, testosterone 17β-dehydrogenase,testosterone 17β-dehydrogenase (NADP⁺), pyridoxine 4-dehydrogenase,ω-hydroxydecanoate dehydrogenase, mannitol 2-dehydrogenase, gluconate5-dehydrogenase, alcohol dehydrogenase [NAD(P)⁺], glycerol dehydrogenase(NADP⁺), octanol dehydrogenase, (R)-aminopropanal dehydrogenase,(S,S)-butanediol dehydrogenase, lactaldehyde reductase, methylglyoxalreductase (NADH-dependent), glyoxylate reductase (NADP⁺), isopropanoldehydrogenase (NADP⁺), hydroxypyruvate reductase, malate dehydrogenase(NADP⁺), D-malate dehydrogenase (decarboxylating), dimethylmalatedehydrogenase, 3-isopropylmalate dehydrogenase, ketol-acidreductoisomerase, homoisocitrate dehydrogenase,hydroxymethylglutaryl-CoA reductase, aryl-alcohol dehydrogenase,aryl-alcohol dehydrogenase (NADP⁺), oxaloglycolate reductase(decarboxylating), tartrate dehydrogenase, glycerol-3-phosphatedehydrogenase [NAD(P)⁺], phosphoglycerate dehydrogenase,diiodophenylpyruvate reductase, 3-hydroxybenzyl-alcohol dehydrogenase,(R)-2-hydroxy-fatty-acid dehydrogenase, (S)-2-hydroxy-fatty-aciddehydrogenase, 3-oxoacyl-[acyl-carrier-protein] reductase,acylglycerone-phosphate reductase, 3-dehydrosphinganine reductase,L-threonine 3-dehydrogenase, 4-oxoproline reductase, all-trans-retinoldehydrogenase (NAD⁺), pantoate 4-dehydrogenase, pyridoxal4-dehydrogenase, carnitine 3-dehydrogenase, indolelactate dehydrogenase,3-(imidazol-5-yl)lactate dehydrogenase, indanol dehydrogenase, L-xylose1-dehydrogenase, apiose 1-reductase, ribose 1-dehydrogenase (NADP⁺),D-arabinose 1-dehydrogenase, D-arabinose 1-dehydrogenase [NAD(P)⁺],glucose 1-dehydrogenase (NAD⁺), glucose 1-dehydrogenase (NADP⁺),galactose 1-dehydrogenase (NADP⁺), aldose 1-dehydrogenase,D-threo-aldose 1-dehydrogenase, sorbose 5-dehydrogenase (NADP⁺),fructose 5-dehydrogenase (NADP⁺), 2-deoxy-D-gluconate 3-dehydrogenase,2-dehydro-3-deoxy-D-gluconate 6-dehydrogenase,2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase, L-idonate2-dehydrogenase, L-threonate 3-dehydrogenase, 3-dehydro-L-gulonate2-dehydrogenase, mannuronate reductase, GDP-mannose 6-dehydrogenase,dTDP-4-dehydrorhamnose reductase, dTDP-6-deoxy-L-talose 4-dehydrogenase,GDP-6-deoxy-D-talose 4-dehydrogenase, UDP-N-acetylglucosamine6-dehydrogenase, ribitol-5-phosphate 2-dehydrogenase, mannitol2-dehydrogenase (NADP⁺), sorbitol-6-phosphate 2-dehydrogenase,15-hydroxyprostaglandin dehydrogenase (NAD⁺), D-pinitol dehydrogenase,sequoyitol dehydrogenase, perillyl-alcohol dehydrogenase,3β-hydroxy-Δ⁵-steroid dehydrogenase, 11β-hydroxysteroid dehydrogenase,16α-hydroxysteroid dehydrogenase, estradiol 17α-dehydrogenase,20α-hydroxysteroid dehydrogenase, 21-hydroxysteroid dehydrogenase (NAM,21-hydroxysteroid dehydrogenase (NADP⁺), 3α-hydroxy-5β-androstane-17-one3α-dehydrogenase, sepiapterin reductase, ureidoglycolate dehydrogenase,glycerol 2-dehydrogenase (NADP⁺), 3-hydroxybutyryl-CoA dehydrogenase,UDP-N-acetylmuramate dehydrogenase, 7α-hydroxysteroid dehydrogenase,dihydrobunolol dehydrogenase, cholestanetetraol 26-dehydrogenase,erythrulose reductase, cyclopentanol dehydrogenase, hexadecanoldehydrogenase, 2-alkyn-1-ol dehydrogenase, hydroxycyclohexanecarboxylatedehydrogenase, hydroxymalonate dehydrogenase, 2-dehydropantolactonereductase (A-specific), 2-dehydropantoate 2-reductase,3β-hydroxy-4α-methylcholestenecarboxylate 3-dehydrogenase(decarboxylating), 2-oxoadipate reductase, L-rhamnose 1-dehydrogenase,cyclohexane-1,2-diol dehydrogenase, D-xylose 1-dehydrogenase,12α-hydroxysteroid dehydrogenase, glycerol-3-phosphate 1-dehydrogenase(NADP⁺), 3-hydroxy-2-methylbutyryl-CoA dehydrogenase, D-xylose1-dehydrogenase (NADP⁺), cholest-5-ene-3β,7α-diol 3β-dehydrogenase,geraniol dehydrogenase, carbonyl reductase (NADPH), L-glycoldehydrogenase, dTDP-galactose 6-dehydrogenase, GDP-4-dehydro-D-rhamnosereductase, prostaglandin-F synthase, prostaglandin-E₂ 9-reductase,indole-3-acetaldehyde reductase (NADH), indole-3-acetaldehyde reductase(NADPH), long-chain-alcohol dehydrogenase,5-amino-6-(5-phosphoribosylamino)uracil reductase, coniferyl-alcoholdehydrogenase, cinnamyl-alcohol dehydrogenase, 15-hydroxyprostaglandin-Ddehydrogenase (NADP⁺), 15-hydroxyprostaglandin dehydrogenase (NADP⁺),(+)-borneol dehydrogenase, (S)-usnate reductase, aldose-6-phosphatereductase (NADPH), 7β-hydroxysteroid dehydrogenase (NADP⁺),1,3-propanediol dehydrogenase, uronate dehydrogenase, IMP dehydrogenase,tropinone reductase I, (−)-menthol dehydrogenase, (+)-neomentholdehydrogenase, 3(or 17)α-hydroxysteroid dehydrogenase, 3β(or20α)-hydroxysteroid dehydrogenase, long-chain-3-hydroxyacyl-CoAdehydrogenase, 3-oxoacyl-[acyl-carrier-protein] reductase (NADH),3α-hydroxysteroid dehydrogenase (A-specific), 2-dehydropantolactonereductase (B-specific), gluconate 2-dehydrogenase, farnesoldehydrogenase, benzyl-2-methyl-hydroxybutyrate dehydrogenase, morphine6-dehydrogenase, dihydrokaempferol 4-reductase,6-pyruvoyltetrahydropterin 2′-reductase, vomifoliol 4′-dehydrogenase,(R)-4-hydroxyphenyllactate dehydrogenase, isopiperitenol dehydrogenase,mannose-6-phosphate 6-reductase, chlordecone reductase,4-hydroxycyclohexanecarboxylate dehydrogenase, (−)-borneoldehydrogenase, (+)-sabinol dehydrogenase, diethyl2-methyl-3-oxosuccinate reductase, 3α-hydroxyglycyrrhetinatedehydrogenase, 15-hydroxyprostaglandin-1 dehydrogenase (NADP⁺),15-hydroxyicosatetraenoate dehydrogenase, N-acylmannosamine1-dehydrogenase, flavanone 4-reductase, 8-oxocoformycin reductase,tropinone reductase II, hydroxyphenylpyruvate reductase,12β-hydroxysteroid dehydrogenase, 3α(17β)-hydroxysteroid dehydrogenase(NAD⁺), N-acetylhexosamine 1-dehydrogenase, 6-endo-hydroxycineoledehydrogenase, carveol dehydrogenase, methanol dehydrogenase,cyclohexanol dehydrogenase, pterocarpin synthase, codeinone reductase(NADPH), salutaridine reductase (NADPH), D-arabinitol 2-dehydrogenase,galactitol-1-phosphate 5-dehydrogenase, tetrahydroxynaphthalenereductase, (S)-carnitine 3-dehydrogenase, mannitol dehydrogenase,fluoren-9-ol dehydrogenase, 4-(hydroxymethyl)benzenesulfonatedehydrogenase, 6-hydroxyhexanoate dehydrogenase, 3-hydroxypimeloyl-CoAdehydrogenase, sulcatone reductase, sn-glycerol-1-phosphatedehydrogenase, 4-hydroxythreonine-4-phosphate dehydrogenase,1,5-anhydro-D-fructose reductase, L-idonate 5-dehydrogenase,3-methylbutanal reductase, dTDP-4-dehydro-6-deoxyglucose reductase,1-deoxy-D-xylulose-5-phosphate reductoisomerase, 2-(R)-hydroxypropyl-CoMdehydrogenase, 2-(S)-hydroxypropyl-CoM dehydrogenase, 3-keto-steroidreductase, GDP-L-fucose synthase, (R)-2-hydroxyacid dehydrogenase,vellosimine dehydrogenase, 2,5-didehydrogluconate reductase,(+)-trans-carveol dehydrogenase, serine 3-dehydrogenase,3β-hydroxy-5β-steroid dehydrogenase, 3β-hydroxy-5α-steroiddehydrogenase, (R)-3-hydroxyacid ester dehydrogenase, (S)-3-hydroxyacidester dehydrogenase, GDP-4-dehydro-6-deoxy-D-mannose reductase,quinate/shikimate dehydrogenase, methylglyoxal reductase(NADPH-dependent), S-(hydroxymethyl)glutathione dehydrogenase,3″-deamino-3″-oxonicotianamine reductase, isocitrate—homoisocitratedehydrogenase, D-arabinitol dehydrogenase (NADP⁺), xanthoxindehydrogenase, sorbose reductase, 4-phosphoerythronate dehydrogenase,2-hydroxymethylglutarate dehydrogenase, 1,5-anhydro-D-fructose reductase(1,5-anhydro-D-mannitol-forming), chlorophyll(ide) b reductase,momilactone-A synthase, dihydrocarveol dehydrogenase, limonene-1,2-dioldehydrogenase, 3-hydroxypropionate dehydrogenase (NADP⁺), malatedehydrogenase [NAD(P)⁺], NADP-retinol dehydrogenase,D-arabitol-phosphate dehydrogenase,2,5-diamino-6-(ribosylamino)-4(3H)-pyrimidinone 5′-phosphate reductase,diacetyl reductase [(R)-acetoin forming], diacetyl reductase[(S)-acetoin forming], UDP-glucuronic acid dehydrogenase(UDP-4-keto-hexauronic acid decarboxylating), S-(hydroxymethyl)mycothioldehydrogenase, D-xylose reductase, phosphonoacetaldehyde reductase(NADH), sulfopropanediol 3-dehydrogenase, (S)-sulfolactatedehydrogenase, (S)-1-phenylethanol dehydrogenase,2-hydroxy-4-carboxymuconate semialdehyde hemiacetal dehydrogenase,sulfoacetaldehyde reductase, germacrene A alcohol dehydrogenase, and11-cis-retinol dehydrogenase); or with a cytochrome as acceptor(including mannitol dehydrogenase (cytochrome), L-lactate dehydrogenase(cytochrome), D-lactate dehydrogenase (cytochrome), D-lactatedehydrogenase (cytochrome c-553), polyvinyl alcohol dehydrogenase(cytochrome), methanol dehydrogenase (cytochrome c), and alcoholdehydrogenase (cytochrome c)); or with oxygen as acceptor (includingmalate oxidase, glucose oxidase, hexose oxidase, cholesterol oxidase,aryl-alcohol oxidase, L-gulonolactone oxidase, galactose oxidase,pyranose oxidase, L-sorbose oxidase, pyridoxine 4-oxidase, alcoholoxidase, catechol oxidase (dimerizing), (S)-2-hydroxy-acid oxidase,ecdysone oxidase, choline oxidase, secondary-alcohol oxidase,4-hydroxymandelate oxidase, long-chain-alcohol oxidase,glycerol-3-phosphate oxidase, thiamin oxidase, hydroxyphytanate oxidase,nucleoside oxidase, N-acylhexosamine oxidase, polyvinyl-alcohol oxidase,D-arabinono-1,4-lactone oxidase, vanillyl-alcohol oxidase, nucleosideoxidase (H₂O₂-forming), and D-mannitol oxidase, alditol oxidase); orwith a disulfide as acceptor (including vitamin-K-epoxide reductase(warfarin-sensitive) or vitamin-K-epoxide reductase(warfarin-insensitive)); or with a quinone or similar compound asacceptor (including quinoprotein glucose dehydrogenase,glycerol-3-phosphate dehydrogenase, malate dehydrogenase (quinone),alcohol dehydrogenase (quinone), formate dehydrogenase-N, cyclic alcoholdehydrogenase (quinone), and quinate dehydrogenase (quinine)); or withother, known, acceptors (including alcohol dehydrogenase (azurin) andglucose-6-phosphate dehydrogenase (coenzyme-F₄₂₀)); or with otheracceptors (including choline dehydrogenase, 2-hydroxyglutaratedehydrogenase, gluconate 2-dehydrogenase (acceptor), dehydrogluconatedehydrogenase, D-2-hydroxy-acid dehydrogenase, lactate—malatetranshydrogenase, pyridoxine 5-dehydrogenase, glucose dehydrogenase(acceptor), fructose 5-dehydrogenase, sorbose dehydrogenase, glucoside3-dehydrogenase, glycolate dehydrogenase, cellobiose dehydrogenase(acceptor), alkan-1-ol dehydrogenase (acceptor), D-sorbitoldehydrogenase (acceptor), glycerol dehydrogenase (acceptor),hydroxyacid-oxoacid transhydrogenase, 3-hydroxycyclohexanonedehydrogenase, (R)-pantolactone dehydrogenase (flavin), glucose-fructoseoxidoreductase, pyranose dehydrogenase (acceptor), 2-oxoacid reductase,(S)-mandelate dehydrogenase, L-sorbose 1-dehydrogenase, formatedehydrogenase (acceptor), soluble quinoprotein glucose dehydrogenase,NDMA-dependent alcohol dehydrogenase, and NDMA-dependent methanoldehydrogenase).

The oxidoreductases which act on the aldehyde or oxo group of donors caninclude, but are not limited to, those with NAD+ or NADP+ as acceptor(including formate dehydrogenase, aldehyde dehydrogenase (NAM, aldehydedehydrogenase (NADP⁺), aldehyde dehydrogenase [NAD(P)⁺], benzaldehydedehydrogenase (NADP⁺), betaine-aldehyde dehydrogenase,glyceraldehyde-3-phosphate dehydrogenase (NADP⁺), acetaldehydedehydrogenase (acetylating), aspartate-semialdehyde dehydrogenase,glyceraldehyde-3-phosphate dehydrogenase (phosphorylating),glyceraldehyde-3-phosphate dehydrogenase (NADP⁺) (phosphorylating),malonate-semialdehyde dehydrogenase, succinate-semialdehydedehydrogenase [NAD(P)⁺], glyoxylate dehydrogenase (acylating),malonate-semialdehyde dehydrogenase (acetylating), aminobutyraldehydedehydrogenase, glutarate-semialdehyde dehydrogenase, glycolaldehydedehydrogenase, lactaldehyde dehydrogenase, 2-oxoaldehyde dehydrogenase(NAM, succinate-semialdehyde dehydrogenase (NAM, 2-oxoisovaleratedehydrogenase (acylating), 2,5-dioxovalerate dehydrogenase,methylmalonate-semialdehyde dehydrogenase (acylating), benzaldehydedehydrogenase (NAM, aryl-aldehyde dehydrogenase, aryl-aldehydedehydrogenase (NADP⁺), L-aminoadipate-semialdehyde dehydrogenase,aminomuconate-semialdehyde dehydrogenase, (R)-dehydropantoatedehydrogenase, retinal dehydrogenase, N-acetyl-γ-glutamyl-phosphatereductase, phenylacetaldehyde dehydrogenase,3α,7α,12α-trihydroxycholestan-26-al 26-oxidoreductase,glutamate-5-semialdehyde dehydrogenase, hexadecanal dehydrogenase(acylating), formate dehydrogenase (NADP⁺), cinnamoyl-CoA reductase,formaldehyde dehydrogenase, 4-trimethylammoniobutyraldehydedehydrogenase, long-chain-aldehyde dehydrogenase, 2-oxoaldehydedehydrogenase (NADP⁺), long-chain-fatty-acyl-CoA reductase, pyruvatedehydrogenase (NADP⁺), oxoglutarate dehydrogenase (NADP⁺),4-hydroxyphenylacetaldehyde dehydrogenase, γ-guanidinobutyraldehydedehydrogenase, butanal dehydrogenase, phenylglyoxylate dehydrogenase(acylating), glyceraldehyde-3-phosphate dehydrogenase (NAD(P)⁺)(phosphorylating), 5-carboxymethyl-2-hydroxymuconic-semialdehydedehydrogenase, 4-hydroxymuconic semialdehyde dehydrogenase,4-formylbenzenesulfonate dehydrogenase, 6-oxohexanoate dehydrogenase,4-hydroxybenzaldehyde dehydrogenase, salicylaldehyde dehydrogenase,vanillin dehydrogenase, coniferyl-aldehyde dehydrogenase,fluoroacetaldehyde dehydrogenase, glutamyl-tRNA reductase,succinylglutamate-semialdehyde dehydrogenase, erythrose-4-phosphatedehydrogenase, sulfoacetaldehyde dehydrogenase, abietadienaldehydrogenase, malonyl CoA reductase (malonate semialdehyde-forming),succinate-semialdehyde dehydrogenase (acetylating),3,4-dehydroadipyl-CoA semialdehyde dehydrogenase (NADP⁺),2-formylbenzoate dehydrogenase, succinate-semialdehyde dehydrogenase(NADP⁺), long-chain acyl-[acyl-carrier-protein] reductase,sulfoacetaldehyde dehydrogenase (acylating), and β-apo-4′-carotenaloxygenase); or with a cytochrome as acceptor (including formatedehydrogenase (cytochrome), formate dehydrogenase (cytochrome-c-553),and carbon-monoxide dehydrogenase (cytochrome-b-561)); or with oxygen asacceptor (including aldehyde oxidase, pyruvate oxidase, oxalate oxidase,glyoxylate oxidase, pyruvate oxidase (CoA-acetylating),indole-3-acetaldehyde oxidase, pyridoxal oxidase, aryl-aldehyde oxidase,retinal oxidase, 4-hydroxyphenylpyruvate oxidase, and abscisic aldehydeoxidase); or with a disulfide as acceptor (including pyruvatedehydrogenase (acetyl-transferring), oxoglutarate dehydrogenase(succinyl-transferring), and 3-methyl-2-oxobutanoate dehydrogenase(2-methylpropanoyl-transferring)); or with a quinone or similar compoundas acceptor (including pyruvate dehydrogenase (quinone)); or with aniron-sulfur protein as acceptor (including pyruvate synthase,2-oxobutyrate synthase, 2-oxoglutarate synthase, carbon-monoxidedehydrogenase (ferredoxin), aldehyde ferredoxin oxidoreductase,glyceraldehyde-3-phosphate dehydrogenase (ferredoxin),3-methyl-2-oxobutanoate dehydrogenase (ferredoxin), indolepyruvateferredoxin oxidoreductase, and oxalate oxidoreductase); or with otheracceptors (including carbon-monoxide dehydrogenase (acceptor), aldehydedehydrogenase (pyrroloquinoline-quinone), formaldehyde dismutase,formylmethanofuran dehydrogenase, carboxylate reductase, and aldehydedehydrogenase (FAD-independent)).

The oxidoreductases which act on the CH—CH group of donors can include,but are not limited to, those with NAD+ or NADP+ as acceptor (e.g.,dihydropyrimidine dehydrogenase (NAD⁺), dihydropyrimidine dehydrogenase(NADP⁺), Δ⁴-3-oxosteroid 5β-reductase, cortisone α-reductase,cucurbitacin Δ²³-reductase, fumarate reductase (NADH), meso-tartratedehydrogenase, acyl-CoA dehydrogenase (NADP⁺),enoyl-[acyl-carrier-protein] reductase (NADH),enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific), 2-coumaratereductase, prephenate dehydrogenase, prephenate dehydrogenase (NADP⁺),dihydroorotate dehydrogenase (NAM, dihydroorotate dehydrogenase (NADP⁺),β-nitroacrylate reductase, 3-methyleneoxindole reductase,kynurenate-7,8-dihydrodiol dehydrogenase,cis-1,2-dihydrobenzene-1,2-diol dehydrogenase,trans-1,2-dihydrobenzene-1,2-diol dehydrogenase, 7-dehydrocholesterolreductase, cholestenone 5α-reductase, biliverdin reductase,1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase,dihydrodipicolinate reductase, 2-hexadecenal reductase,2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase,cis-1,2-dihydro-1,2-dihydroxynaphthalene dehydrogenase, progesterone5α-reductase, 2-enoate reductase, maleylacetate reductase,protochlorophyllide reductase, 2,4-dienoyl-CoA reductase (NADPH),phosphatidylcholine desaturase, geissoschizine dehydrogenase,cis-2-enoyl-CoA reductase (NADPH), trans-2-enoyl-CoA reductase (NADPH),enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific),2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate reductase, xanthommatinreductase, 12-oxophytodienoate reductase, arogenate dehydrogenase,trans-2-enoyl-CoA reductase (NAD⁺), 2′-hydroxyisoflavone reductase,biochanin-A reductase, α-santonin 1,2-reductase, 15-oxoprostaglandin13-oxidase, cis-3,4-dihydrophenanthrene-3,4-diol dehydrogenase,2′-hydroxydaidzein reductase, 2-methyl-branched-chain-enoyl-CoAreductase, (3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylatedehydrogenase, precorrin-6A reductase, cis-2,3-dihydrobiphenyl-2,3-dioldehydrogenase, phloroglucinol reductase,2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase, dibenzothiophenedihydrodiol dehydrogenase, terephthalate 1,2-cis-dihydrodioldehydrogenase, pimeloyl-CoA dehydrogenase, 2,4-dichlorobenzoyl-CoAreductase, phthalate 4,5-cis-dihydrodiol dehydrogenase,5,6-dihydroxy-3-methyl-2-oxo-1,2,5,6-tetrahydroquinoline dehydrogenase,cis-dihydroethylcatechol dehydrogenase,cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylatedehydrogenase, 1,2-dihydroxy-6-methylcyclohexa-3,5-dienecarboxylatedehydrogenase, zeatin reductase, Δ¹⁴-sterol reductase, Δ²⁴⁽²⁴¹⁾-sterolreductase, Δ²⁴-sterol reductase, 1,2-dihydrovomilenine reductase,2-alkenal reductase, divinyl chlorophyllide a 8-vinyl-reductase,precorrin-2 dehydrogenase, anthocyanidin reductase, arogenatedehydrogenase (NADP⁺), arogenate dehydrogenase [NAD(P)⁺], redchlorophyll catabolite reductase, (+)-pulegone reductase,(−)-isopiperitenone reductase, geranylgeranyl diphosphate reductaseacrylyl-CoA reductase (NADPH), crotonyl-CoA carboxylase/reductase,crotonyl-CoA reductase,3-(cis-5,6-dihydroxycyclohexa-1,3-dien-l-yl)propanoate dehydrogenase,tRNA-dihydrouridine^(16/17) synthase [NAD(P)⁺], tRNA-dihydrouridine⁴⁷synthase [NAD(P)⁺], tRNA-dihydrouridine^(20a/20b) synthase [NAD(P)⁺],and tRNA-dihydrouridine²⁰ synthase [NAD(P)⁺]) or with a cytochrome asacceptor, e.g. L-galactonolactone dehydrogenase, or with oxygen asacceptor (e.g., coproporphyrinogen oxidase, protoporphyrinogen oxidase,bilirubin oxidase, acyl-CoA oxidase, dihydrouracil oxidase,tetrahydroberberine oxidase, secologanin synthase, tryptophanα,β-oxidase, pyrroloquinoline-quinone synthase, and L-galactonolactoneoxidase), or with a quinine or related compound as acceptor (e.g.,succinate dehydrogenase (ubiquinone), dihydroorotate dehydrogenase(quinone), protoporphyrinogen IX dehydrogenase (menaquinone), fumaratereductase (menaquinone), 15-cis-phytoene desaturase, and9,9′-dicis-ζ-carotene desaturase), or with an iron-sulfur protein asacceptor (e.g., 6-hydroxynicotinate reductase,15,16-dihydrobiliverdin:ferredoxin oxidoreductase,phycoerythrobilin:ferredoxin oxidoreductase, phytochromobilin:ferredoxinoxidoreductase, phycocyanobilin:ferredoxin oxidoreductase,phycoerythrobilin synthase, ferredoxin:protochlorophyllide reductase(ATP-dependent), benzoyl-CoA reductase, and 4-hydroxybenzoyl-CoAreductase) or with flavin as acceptor (e.g., butyryl-CoA dehydrogenaseor 4,4′-diapophytoene desaturase), or with other, known acceptors (e.g.,dihydroorotate dehydrogenase (fumarate)), or with other acceptors (e.g.,succinate dehydrogenase, acyl-CoA dehydrogenase, 3-oxosteroid1-dehydrogenase, 3-oxo-5α-steroid 4-dehydrogenase, 3-oxo-5β-steroid4-dehydrogenase, glutaryl-CoA dehydrogenase, 2-furoyl-CoA dehydrogenase,isovaleryl-CoA dehydrogenase, 2-methylacyl-CoA dehydrogenase,long-chain-acyl-CoA dehydrogenase, cyclohexanone dehydrogenase,isoquinoline 1-oxidoreductase, quinoline 2-oxidoreductase, quinaldate4-oxidoreductase, quinoline-4-carboxylate 2-oxidoreductase,(R)-benzylsuccinyl-CoA dehydrogenase, coproporphyrinogen dehydrogenase,all-trans-retinol 13,14-reductase, 2-amino-4-deoxychorismatedehydrogenase, carvone reductase, all-trans-ζ-carotene desaturase,1-hydroxycarotenoid 3,4-desaturase, phytoene desaturase(neurosporene-forming), phytoene desaturase (ζ-carotene-forming),phytoene desaturase (3,4-didehydrolycopene-forming), and phytoenedesaturase (lycopene-forming)).

The oxidoreductases which act on the CH—NH2 group of donors can include,but are not limited to, those with NAD⁺ or NADP⁺ as acceptor (e.g.,alanine dehydrogenase, glutamate dehydrogenase, glutamate dehydrogenase[NAD(P)⁺], glutamate dehydrogenase (NADP⁺), L-amino-acid dehydrogenase,serine 2-dehydrogenase, valine dehydrogenase (NADP⁺), leucinedehydrogenase, glycine dehydrogenase, L-erythro-3,5-diaminohexanoatedehydrogenase, 2,4-diaminopentanoate dehydrogenase, glutamate synthase(NADPH), glutamate synthase (NADH), lysine dehydrogenase,diaminopimelate dehydrogenase, N-methylalanine dehydrogenase, lysine6-dehydrogenase, tryptophan dehydrogenase, phenylalanine dehydrogenase,and aspartate dehydrogenase), or with a chyochrome as acceptor (e.g.glycine dehydrogenase (cytochrome)), or with oxygen as acceptor (e.g.D-aspartate oxidase, L-amino-acid oxidase, D-amino-acid oxidase, amineoxidase, pyridoxal 5′-phosphate synthase, D-glutamate oxidase,ethanolamine oxidase, putrescine oxidase, L-glutamate oxidase,cyclohexylamine oxidase, protein-lysine 6-oxidase, L-lysine oxidase,D-glutamate(D-aspartate) oxidase, L-aspartate oxidase, glycine oxidase,L-lysine 6-oxidase, primary-amine oxidase, diamine oxidase, and7-chloro-L-tryptophan oxidase), or with a disulfide as acceptor (e.g.glycine dehydrogenase (decarboxylating)), or with a quinine or similarcompound as acceptor (e.g. D-amino acid dehydrogenase (quinone)) or withan iron-sulfur protein as acceptor (e.g. glutamate synthase(ferredoxin)), or with a copper protein as acceptor (e.g. methylaminedehydrogenase (amicyanin) and aralkylamine dehydrogenase (azurin)), andwith other acceptors (e.g D-amino-acid dehydrogenase, taurinedehydrogenase, and glycine dehydrogenase (cyanide-forming)).

The oxidoreductases which act on the CH-NH group of donors can include,but are not limited to, those with NAD⁺ or NADP⁺ as acceptor (e.g.,pyrroline-2-carboxylate reductase, pyrroline-5-carboxylate reductase,dihydrofolate reductase, methylenetetrahydrofolate dehydrogenase(NADP⁺), formyltetrahydrofolate dehydrogenase, saccharopinedehydrogenase (NAD⁺, L-lysine-forming), saccharopine dehydrogenase(NADP⁺, L-lysine-forming), saccharopine dehydrogenase (NAD⁺,L-glutamate-forming), saccharopine dehydrogenase (NADP⁺,L-glutamate-forming), D-octopine dehydrogenase,1-pyrroline-5-carboxylate dehydrogenase, methylenetetrahydrofolatedehydrogenase (NAD⁺), D-lysopine dehydrogenase, alanopine dehydrogenase,ephedrine dehydrogenase, D-nopaline dehydrogenase,methylenetetrahydrofolate reductase [NAD(P)H],Δ¹-piperideine-2-carboxylate reductase, strombine dehydrogenase,tauropine dehydrogenase, N⁵-(carboxyethyl)ornithine synthase,thiomorpholine-carboxylate dehydrogenase, β-alanopine dehydrogenase,1,2-dehydroreticulinium reductase (NADPH), opine dehydrogenase, flavinreductase (NADPH), berberine reductase, vomilenine reductase, pteridinereductase, 6,7-dihydropteridine reductase, flavin reductase (NADH), FADreductase (NADH), FMN reductase (NADPH), FMN reductase [NAD(P)H],8-hydroxy-5-deazaflavin:NADPH oxidoreductase, riboflavin reductase[NAD(P)H], and FMN reductase (NADH)), with oxygen as acceptor (e.g.,sarcosine oxidase, N-methyl-L-amino-acid oxidase, N⁶-methyl-lysineoxidase, (S)-6-hydroxynicotine oxidase, (R)-6-hydroxynicotine oxidase,L-pipecolate oxidase, dimethylglycine oxidase,dihydrobenzophenanthridine oxidase, N¹-acetylpolyamine oxidase,polyamine oxidase (propane-1,3-diamine-forming), N^(th)-acetylspermidine oxidase (propane-1,3-diamine-forming), spermineoxidase, non-specific polyamine oxidase, and L-saccharopine oxidase),with a disulfide as acceptor (e.g. pyrimidodiazepine synthase), with aquinine or similar compound as acceptor (e.g.electron-transferring-flavoprotein dehydrogenase), with an iron-sulfurprotein as acceptor (e.g. methylenetetrahydrofolate reductase(ferredoxin)), with a flavin as acceptor (e.g. dimethylaminedehydrogenase, and trimethylamine dehydrogenase), and with otheracceptors (e.g., sarcosine dehydrogenase, dimethylglycine dehydrogenase,L-pipecolate dehydrogenase, nicotine dehydrogenase, methylglutamatedehydrogenase, spermidine dehydrogenase, proline dehydrogenase,methylenetetrahydromethanopterin dehydrogenase,5,10-methylenetetrahydromethanopterin reductase, cytokinindehydrogenase, and D-proline dehydrogenase).

The oxidoreductases which act on NADH or NADPH can include, but are notlimited to, those with NAD or NADP as acceptor (e.g., NAD(P)⁺transhydrogenase (B-specific), and NAD(P)⁺ transhydrogenase(AB-specific)), with a heme protein as acceptor (e.g. cytochrome-b₅reductase, NADPH—hemoprotein reductase, NADPH—cytochrome-c₂ reductase,and leghemoglobin reductase), with oxygen as acceptor (e.g. NAD(P)Hoxidase), with a quinine or similar compound as acceptor (e.g., NAD(P)Hdehydrogenase (quinone), NADH:ubiquinone reductase (H⁺-translocating),monodehydroascorbate reductase (NADH), NADPH:quinone reductase,p-benzoquinone reductase (NADPH), 2-hydroxy-1,4-benzoquinone reductase,NADH:ubiquinone reductase (Nat-transporting), NADH:ubiquinone reductase(non-electrogenic), and NADPH dehydrogenase (quinone)), with anitrogenous group as acceptor (e.g. trimethylamine-N-oxide reductase),with an iron-sulfur protein as acceptor, with a flavin as acceptor, andwith other acceptors (e.g, NADPH dehydrogenase, NADH dehydrogenase, NADHdehydrogenase (quinone)).

The oxidoreductases which act on other nitrogenous compounds as donorscan include, but are not limited to, those with NAD or NADP as acceptor(e.g., nitrate reductase (NADH), nitrate reductase [NAD(P)H], nitratereductase (NADPH), nitrite reductase [NAD(P)H], hyponitrite reductase,azobenzene reductase, GMP reductase, nitroquinoline-N-oxide reductase,hydroxylamine reductase (NADH), 4-(dimethylamino)phenylazoxybenzenereductase, N-hydroxy-2-acetamidofluorene reductase, preQ₁ reductase, andnitric oxide reductase [NAD(P), nitrous oxide-forming]), with acytochrome as acceptor (e.g. nitrite reductase (NO-forming), nitritereductase (cytochrome; ammonia-forming), trimethylamine-N-oxidereductase (cytochrome c), nitrous-oxide reductase, and nitric oxidereductase (cytochrome c)), with oxygen as acceptor (e.g., nitroalkaneoxidase, acetylindoxyl oxidase, factor-independent urate hydroxylase,hydroxylamine oxidase, and 3-aci-nitropropanoate oxidase), with aquinone or similar compound as acceptor (e.g. nitrate reductase(quinone) and nitric oxide reductase (menaquinol)), with a nitrogenousgroup as acceptor (e.g. nitrite dismutase), with an iron-sulfur proteinas acceptor (e.g, ferredoxin—nitrite reductase and ferredoxin—nitratereductase), and with other acceptors (e.g., hydroxylamine reductase,nitrate reductase, and hydrazine oxidoreductase).

The oxidoreductases which act on a sulfur group of donors can include,but are not limited to, those with NAD or NADP as acceptor (e.g.,sulfite reductase (NADPH), hypotaurine dehydrogenase, dihydrolipoyldehydrogenase, 2-oxopropyl-CoM reductase (carboxylating) , cystinereductase, glutathione-disulfide reductase, protein-disulfide reductase,thioredoxin-disulfide reductase, CoA-glutathione reductase, asparagusatereductase, trypanothione-disulfide reductase, bis-γ-glutamylcystinereductase, CoA-disulfide reductase, mycothione reductase, glutathioneamide reductase, and dimethylsulfone reductase), with a cytochrome asacceptor (e.g., sulfite dehydrogenase, thiosulfate dehydrogenasesulfide-cytochrome-c reductase (flavocytochrome c), and dimethylsulfide:cytochrome c₂ reductase), with oxygen as acceptor (e.g. sulfiteoxidase, thiol oxidase, glutathione oxidase, methanethiol oxidase,prenylcysteine oxidase, and farnesylcysteine lyase), with a disulfide asacceptor (e.g., glutathione—homocystine transhydrogenase,protein-disulfide reductase (glutathione), glutathione—CoA-glutathionetranshydrogenase, glutathione—cystine transhydrogenase, enzyme-thioltranshydrogenase (glutathione-disulfide), phosphoadenylyl-sulfatereductase (thioredoxin), adenylyl-sulfate reductase (glutathione),adenylyl-sulfate reductase (thioredoxin), peptide-methionine (S)-S-oxidereductase, peptide-methionine (R)-S-oxide reductase, L-methionine(S)-S-oxide reductase, and L-methionine (R)-S-oxide reductase), with aquinine or similar compound as acceptor (e.g., glutathione dehydrogenase(ascorbate), thiosulfate dehydrogenase (quinone), dimethylsulfoxidereductase, and sulfide:quinone reductase), with a nitrogenous group asacceptor, with an iron-sulfur protein as acceptor (e.g. sulfitereductase (ferredoxin) and ferredoxin:thioredoxin reductase), withother, known acceptors (e.g. CoB—CoM heterodisulfide reductase andsulfiredoxin), and with other acceptors (e.g. sulfite reductase,adenylyl-sulfate reductase, and hydrogensulfite reductase).

The oxidoreductases which act on a heme group of donors can include, butare not limited to, those with oxygen as acceptor (e.g., cytochrome-coxidase), with a nitrogenous group as acceptor (e.g. nitrate reductase(cytochrome)), and with other acceptors (e.g. iron—cytochrome-creductase).

The oxidoreductases which act on diphenols and related substances asdonors can include, but are not limited to, those with NAD or NADP asacceptor (e.g. trans-acenaphthene-1,2-diol dehydrogenase), with acytochrome as acceptor (e.g. L-ascorbate—cytochrome-b₅reductase andubiquinol—cytochrome-c reductase), with oxygen as acceptor (e.g,catechol oxidase, laccase, L-ascorbate oxidase, o-aminophenol oxidase,3-hydroxyanthranilate oxidase, rifamycin-B oxidase, photosystem II,ubiquinol oxidase (H⁺-transporting), ubiquinol oxidase, and menaquinoloxidase (H⁺-transporting)), and with other acceptors (e.g.,plastoquinol—plastocyanin reductase, ribosyldihydronicotinamidedehydrogenase (quinone), and violaxanthin de-epoxidase).

The oxidoreductases which act on peroxide as acceptor can include, butare not limited to, peroxidases (e.g., NADH peroxidase, NADPHperoxidase, fatty-acid peroxidase, cytochrome-c peroxidase, catalase,peroxidase, iodide peroxidase, glutathione peroxidase, chlorideperoxidase, L-ascorbate peroxidase, phospholipid-hydroperoxideglutathione peroxidase, manganese peroxidase, lignin peroxidase,peroxiredoxin, versatile peroxidase, glutathione amide-dependentperoxidase, bromide peroxidase, dye decolorizing peroxidase ,prostamide/prostaglandin F_(2α) synthase, catalase-peroxidase) and thosewith H₂O₂ as acceptor, one oxygen atom of which is incorporated into theproduct (e.g. unspecific peroxygenase, myeloperoxidase, plant seedperoxygenase, and fatty-acid peroxygenase).

The oxidoreductases which act on hydrogen as donor can include, but arenot limited to, those with NAD or NADP as acceptor (e.g., hydrogendehydrogenase, hydrogen dehydrogenase (NADP⁺), and hydrogenase (NAD⁺,ferredoxin)), with a cytochrome as acceptor (e.g. cytochrome-c₃hydrogenase), with a quinine or similar compound as acceptor (e.g.,hydrogen:quinone oxidoreductase), with an iron-sulfur protein asacceptor (e.g. ferredoxin hydrogenase), with other known acceptors(e.g., coenzyme F₄₂₀ hydrogenase, 5,10-methenyltetrahydromethanopterinhydrogenase, and Methanosarcina-phenazine hydrogenase), and with otheracceptors (e.g. hydrogenase (acceptor)).

The oxidoreductases which act on single donors with incorporation ofmolecular oxygen (oxygenases) can include, but are not limited to, thosewith incorporation of two atoms of oxygen (e.g., catechol1,2-dioxygenase, catechol 2,3-dioxygenase, protocatechuate3,4-dioxygenase, gentisate 1,2-dioxygenase, homogentisate1,2-dioxygenase, 3-hydroxyanthranilate 3,4-dioxygenase, protocatechuate4,5-dioxygenase, 2,5-dihydroxypyridine 5,6-dioxygenase,7,8-dihydroxykynurenate 8,8a-dioxygenase, tryptophan 2,3-dioxygenase,linoleate 13S-lipoxygenase, ascorbate 2,3-dioxygenase,2,3-dihydroxybenzoate 3,4-dioxygenase, 3,4-dihydroxyphenylacetate2,3-dioxygenase, 3-carboxyethylcatechol 2,3-dioxygenase, indole2,3-dioxygenase, sulfur dioxygenase, cysteamine dioxygenase, cysteinedioxygenase, caffeate 3,4-dioxygenase, 2,3-dihydroxyindole2,3-dioxygenase, quercetin 2,3-dioxygenase,3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione4,5-dioxygenase, peptide-tryptophan 2,3-dioxygenase,4-hydroxyphenylpyruvate dioxygenase, 2,3-dihydroxybenzoate2,3-dioxygenase, stizolobate synthase, stizolobinate synthase,arachidonate 12-lipoxygenase, arachidonate 15-lipoxygenase, arachidonate5-lipoxygenase, pyrogallol 1,2-oxygenase, chloridazon-catecholdioxygenase, hydroxyquinol 1,2-dioxygenase, 1-hydroxy-2-naphthoate1,2-dioxygenase, biphenyl-2,3-diol 1,2-dioxygenase, arachidonate8-lipoxygenase, 2,4′-dihydroxyacetophenone dioxygenase, lignostilbeneαβ-dioxygenase, linoleate diol synthase, linoleate 11-lipoxygenase ,4-hydroxymandelate synthase, 3-hydroxy-4-oxoquinoline 2,4-dioxygenase,3-hydroxy-2-methyl-quinolin-4-one 2,4-dioxygenase, chlorite O₂-lyase,acetylacetone-cleaving enzyme, 9-cis-epoxycarotenoid dioxygenase,indoleamine 2,3-dioxygenase, acireductone dioxygenase (Ni²⁺-requiring),acireductone dioxygenase [iron(II)-requiring], sulfuroxygenase/reductase, 1,2-dihydroxynaphthalene dioxygenase, gallatedioxygenase, linoleate 9S-lipoxygenase, and torulene dioxygenase), withincorporation of one atom of oxygen (internal monooxygenases or internalmixed function oxidases) (e.g., arginine 2-monooxygenase, lysine2-monooxygenase, tryptophan 2-monooxygenase, lactate 2-monooxygenase,Renilla-luciferin 2-monooxygenase, Cypridina-luciferin 2-monooxygenase,Photinus-luciferin 4-monooxygenase (ATP-hydrolysing),Watasenia-luciferin 2-monooxygenase, phenylalanine 2-monooxygenase,apo-β-carotenoid-14′,13′-dioxygenase, Oplophorus-luciferin2-monooxygenase, 3,4-dihydroxyphenylalanine oxidative deaminase,nitronate monooxygenase , dichloroarcyriaflavin A synthase,dinoflagellate luciferase, and 2-oxuglutarate dioxygenase(ethylene-forming)), inositol oxygenase, and tryptophan 2′-dioxygenase.

The oxidoreductases which act on paired donors, with incorporation orreduction of molecular oxygen can include, but are not limited to, thosewith ascorbate as one donor, with reduced pteridine as one donor, with2-oxoglutarate as one donor, and incorporation of one atom each ofoxygen into both donors (e.g. γ-butyrobetaine dioxygenase,procollagen-proline dioxygenase, pyrimidine-deoxynucleoside2′-dioxygenase, procollagen-lysine 5-dioxygenase, thymine dioxygenase,procollagen-proline 3-dioxygenase, trimethyllysine dioxygenase,flavanone 3-dioxygenase, pyrimidine-deoxynucleoside 1′-dioxygenase,hyoscyamine (6S)-dioxygenase, gibberellin-44 dioxygenase, gibberellin2β-dioxygenase, 6β-hydroxyhyoscyamine epoxidase, gibberellin3β-dioxygenase, peptide-aspartate β-dioxygenase, taurine dioxygenase,phytanoyl-CoA dioxygenase, leucocyanidin oxygenase, deacetoxyvindoline4-hydroxylase, clavaminate synthase, flavone synthase, flavonolsynthase, 2′-deoxymugineic-acid 2′-dioxygenase, mugineic-acid3-dioxygenase, deacetoxycephalosporin-C hydroxylase,[histone-H3]-lysine-36 demethylase, proline 3-hydroxylase,hypoxia-inducible factor-proline dioxygenase , hypoxia-induciblefactor-asparagine dioxygenase , thebaine 6-O-demethylase, codeine3-O-demethylase, DNA oxidative demethylase, and2-oxoglutarate/L-arginine monooxygenase/decarboxylase(succinate-forming)), with NADH or NADPH as one donor, and incorporationof two atoms of oxygen into one donor (e.g., anthranilate1,2-dioxygenase (deaminating, decarboxylating), benzene 1,2-dioxygenase,3-hydroxy-2-methylpyridinecarboxylate dioxygenase, 5-pyridoxatedioxygenase, phthalate 4,5-dioxygenase, 4-sulfobenzoate 3,4-dioxygenase,4-chlorophenylacetate 3,4-dioxygenase, benzoate 1,2-dioxygenase, toluenedioxygenase, naphthalene 1,2-dioxygenase, 2-chlorobenzoate1,2-dioxygenase, 2-aminobenzenesulfonate 2,3-dioxygenase, terephthalate1,2-dioxygenase, 2-hydroxyquinoline 5,6-dioxygenase, nitric oxidedioxygenase, biphenyl 2,3-dioxygenase, 3-phenylpropionate dioxygenase,pheophorbide a oxygenase, benzoyl-CoA 2,3-dioxygenase, and carbazole1,9α-dioxygenase), with NADH or NADPH as one donor, and incorporation ofone atom of oxygen (e.g., salicylate 1-monooxygenase, 4-hydroxybenzoate3-monooxygenase, melilotate 3-monooxygenase, imidazoleacetate4-monooxygenase, orcinol 2-monooxygenase, phenol 2-monooxygenase,flavin-containing monooxygenase, kynurenine 3-monooxygenase,2,6-dihydroxypyridine 3-monooxygenase, trans-cinnamate 4-monooxygenase,benzoate 4-monooxygenase, calcidiol 1-monooxygenase, trans-cinnamate2-monooxygenase, cholestanetriol 26-monooxygenase, cyclopentanonemonooxygenase, cholesterol 7α-monooxygenase, 4-hydroxyphenylacetate1-monooxygenase, taxifolin 8-monooxygenase, 2,4-dichlorophenol6-monooxygenase, flavonoid 3′-monooxygenase, cyclohexanonemonooxygenase, 3-hydroxybenzoate 4-monooxygenase, 3-hydroxybenzoate6-monooxygenase, methane monooxygenase (soluble), phosphatidylcholine12-monooxygenase, 4-aminobenzoate 1-monooxygenase,3,9-dihydroxypterocarpan 6α-monooxygenase, 4-nitrophenol2-monooxygenase, leukotriene-B₄ 20-monooxygenase, 2-nitrophenol2-monooxygenase, albendazole monooxygenase, 4-hydroxybenzoate3-monooxygenase [NAD(P)H], leukotriene-E₄ 20-monooxygenase, anthranilate3-monooxygenase (deaminating), 5-O-(4-coumaroyl)-D-quinate3′-monooxygenase, methyltetrahydroprotoberberine 14-monooxygenase,anhydrotetracycline monooxygenase, nitric-oxide synthase,anthraniloyl-CoA monooxygenase, tyrosine N-monooxygenase, questinmonooxygenase, 2-hydroxybiphenyl 3-monooxygenase , (−)-mentholmonooxygenase, (S)-limonene 3-monooxygenase, (S)-limonene6-monooxygenase, (S)-limonene 7-monooxygenase, pentachlorophenolmonooxygenase, 6-oxocineole dehydrogenase, isoflavone 3′-hydroxylase,4′-methoxyisoflavone 2′-hydroxylase, ketosteroid monooxygenase,protopine 6-monooxygenase, dihydrosanguinarine 10-monooxygenase,dihydrochelirubine 12-monooxygenase, benzoyl-CoA 3-monooxygenase,L-lysine 6-monooxygenase (NADPH), 27-hydroxycholesterol7α-monooxygenase, 2-hydroxyquinoline 8-monooxygenase, 4-hydroxyquinoline3-monooxygenase, 3-hydroxyphenylacetate 6-hydroxylase, 4-hydroxybenzoate1-hydroxylase, 2-hydroxycyclohexanone 2-monooxygenase, quinine3-monooxygenase, 4-hydroxyphenylacetaldehyde oxime monooxygenase, alkenemonooxygenase, sterol 14-demethylase, N-methylcoclaurine3′-monooxygenase, methylsterol monooxygenase, tabersonine16-hydroxylase, 7-deoxyloganin 7-hydroxylase, vinorine hydroxylase,taxane 10β-hydroxylase, taxane 13α-hydroxylase, ent-kaurene oxidase,ent-kaurenoic acid oxidase, (R)-limonene 6-monooxygenase,magnesium-protoporphyrin IX monomethyl ester (oxidative) cyclase,vanillate monooxygenase, precorrin-3B synthase, 4-hydroxyacetophenonemonooxygenase, glyceollin synthase, 2-hydroxyisoflavanone synthase,licodione synthase, flavonoid 3′,5′-hydroxylase, isoflavone2′-hydroxylase, zeaxanthin epoxidase, deoxysarpagine hydroxylase,phenylacetone monooxygenase, (+)-abscisic acid 8′-hydroxylase,lithocholate 6β-hydroxylase, 7α-hydroxycholest-4-en-3-one12α-hydroxylase, 5β-cholestane-3α,7α-diol 12α-hydroxylase,taurochenodeoxycholate 6α-hydroxylase, cholesterol 24-hydroxylase,24-hydroxycholesterol 7α-hydroxylase, 25-hydroxycholesterol7α-hydroxylase, senecionine N-oxygenase, psoralen synthase,8-dimethylallylnaringenin 2′-hydroxylase, (+)-menthofuran synthase,monocyclic monoterpene ketone monooxygenase, epi-isozizaene5-monooxygenase, limonene 1,2-monooxygenase, abietadiene hydroxylase ,abietadienol hydroxylase , geranylgeraniol 18-hydroxylase ,methanesulfonate monooxygenase, 3-epi-6-deoxocathasterone23-monooxygenase, FAD-dependent urate hydroxylase, 6-hydroxynicotinate3-monooxygenase, angelicin synthase, geranylhydroquinone 3″-hydroxylase,isoleucine N-monooxygenase , valine N-monooxygenase, 5-epiaristolochene1,3-dihydroxylase, costunolide synthase, premnaspirodiene oxygenase,chlorophyllide-α oxygenase, germacrene A hydroxylase, phenylalanineN-monooxygenase, tryptophan N-monooxygenase, vitamin D₃ 24-hydroxylase,3-(3-hydroxyphenyl)propanoate hydroxylase, 7-methylxanthine demethylase,(3-carotene 3-hydroxylase, pyrrole-2-carboxylate monooxygenase,dimethyl-sulfide monooxygenase , and squalene monooxygenase, withreduced flavin or flavoprotein as one donor, and incorporation of oneatom of oxygen (e.g., unspecific monooxygenase, alkanal monooxygenase(FMN-linked), alkanesulfonate monooxygenase, tryptophan 7-halogenase,anthranilate 3-monooxygenase (FAD), 4-hydroxyphenylacetate3-monooxygenase, and nitrilotriacetate monooxygenase), with reducediron-sulfur protein as one donor, and incorporation of one atom ofoxygen (e.g., camphor 5-monooxygenase, camphor 1,2-monooxygenase, alkane1-monooxygenase, steroid 11β-monooxygenase, corticosterone18-monooxygenase, cholesterol monooxygenase (side-chain-cleaving),choline monooxygenase , and steroid 15β-monooxygenase), with reducedpteridine as one donor, and incorporation of one atom of oxygen (e.g.,phenylalanine 4-monooxygenase, tyrosine 3-monooxygenase, anthranilate3-monooxygenase, tryptophan 5-monooxygenase, alkylglycerolmonooxygenase, and mandelate 4-monooxygenase), with reduced ascorbate asone donor, and incorporation of one atom of oxygen (e.g, dopamineβ-monooxygenase, peptidylglycine monooxygenase, andaminocyclopropanecarboxylate oxidase), with another compound as onedonor, and incorporation of one atom of oxygen (e.g., monophenolmonooxygenase, CMP-N-acetylneuraminate monooxygenase, and methanemonooxygenase (particulate)), with oxidation of a pair of donorsresulting in the reduction of molecular oxygen to two molecules of water(e.g., stearoyl-CoA 9-desaturase, acyl-[acyl-carrier-protein] desaturase, linoleoyl-CoA desaturase , Δ⁸-fatty-acid desaturase, Δ¹¹-fatty-aciddesaturase, Δ¹²-fatty-acid desaturase, and (S)-2-hydroxypropylphosphonicacid epoxidase), with 2-oxoglutarate as one donor, and the otherdehydrogenated (e.g. deacetoxycephalosporin-C synthase), with NADH orNADPH as one donor, and the other dehydrogenated (e.g., (S)-stylopinesynthase, (S)-cheilanthifoline synthase, berbamunine synthase,salutaridine synthase, (S)-canadine synthase, lathosterol oxidase,biflaviolin synthase, pseudobaptigenin synthase), and others includingprostaglandin-endoperoxide synthase, kynurenine 7,8-hydroxylase, hemeoxygenase, progesterone monooxygenase, steroid 17α-monooxygenase,steroid 21-monooxygenase, estradiol 6β-monooxygenase,4-androstene-3,β-dione monooxygenase, progesterone 11α-monooxygenase,4-methoxybenzoate monooxygenase (O-demethylating), plasmanylethanolaminedesaturase, phylloquinone monooxygenase (2,3-epoxidizing),Latia-luciferin monooxygenase (demethylating), ecdysone20-monooxygenase, 3-hydroxybenzoate 2-monooxygenase, steroid9α-monooxygenase, 2-hydroxypyridine 5-monooxygenase, juglone3-monooxygenase, linalool 8-monooxygenase, deoxyhypusine monooxygenase,myristoyl-CoA 11-(E) desaturase, myristoyl-CoA 11-(Z) desaturase,Δ¹²-fatty acid dehydrogenase, monoprenyl isoflavone epoxidase ,thiophene-2-carbonyl-CoA monooxygenase, β-carotene 15,15′-monooxygenase,taxadiene 5α-hydroxylase, cholesterol 25-hydroxylase, ammoniamonooxygenase, 5,6-dimethylbenzimidazole synthase,all-trans-8′-apo-β-carotenal 15,15′-oxygenase, zeaxanthin7,8-dioxygenase, β-amyrin 24-hydroxylase, diapolycopene oxygenase, andcarotene ε-monooxygenase.

The oxidoreductases which act on superoxide as acceptor can include, butare not limited to, superoxide dismutase and superoxide reductase.

The oxidoreductases which act on metal ions can include, but are notlimited to, those with NAD⁺ or NADP⁺ as acceptor (e.g., mercury(II)reductase, diferric-transferrin reductase, aquacobalamin reductase,cob(II)alamin reductase, aquacobalamin reductase (NADPH), cyanocobalaminreductase (cyanide-eliminating), ferric-chelate reductase (NADH),[methionine synthase] reductase, and ferric-chelate reductase (NADPH)),with oxygen as acceptor (e.g., ferroxidase), with quinone or similarcompound as acceptor (e.g.ascorbate ferrireductase (transmembrane)),with flavin as acceptor (e.g. cob(II)yrinic acid a,c-diamide reductase),with other acceptors (e.g. iron:rusticyanin reductase).

The oxidoreductases which act on CH or CH₂ groups can include, but arenot limited to, those with NAD⁺ or NADP⁺ as acceptor (e.g.,CDP-4-dehydro-6-deoxyglucose reductase, 4-hydroxy-3-methylbut-2-enyldiphosphate reductase, leucoanthocyanidin reductase, xanthinedehydrogenase, and nicotinate dehydrogenase), with a cytochrome asacceptor (e.g. nicotinate dehydrogenase (cytochrome)), with oxygen asacceptor (e.g., pteridine oxidase, xanthine oxidase, and6-hydroxynicotinate dehydrogenase), with a disulfide as acceptor (e.g.,ribonucleoside-diphosphate reductase, and ribonucleoside-triphosphatereductase), with a quinine or similar compound as acceptor (e.g.,phenylacetyl-CoA dehydrogenase and caffeine dehydrogenase), with aniron-sulfur protein as acceptor (e.g.,(E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase), and with otheracceptors (e.g., 4-methylphenol dehydrogenase (hydroxylating),ethylbenzene hydroxylase, 3α,7α,12α-trihydroxy-5β-cholestanoyl-CoA24-hydroxylase, uracil/thymine dehydrogenase, and bile-acid7α-dehydroxylase).

The oxidoreductases which act on iron-sulfur proteins as donors caninclude, but are not limited to, those with NAD+ or NADP+ as acceptor(e.g., rubredoxin—NAD⁺ reductase, ferredoxin—NADP+ reductase,ferredoxin—NAD+ reductase, and rubredoxin—NAD(P)⁺ reductase), with H⁺ asacceptor, and with dinitrogen as acceptor (e.g., nitrogenase).

The oxidoreductases which act on reduced flavodoxin as donor caninclude, but are not limited to, those with dinitrogen as acceptor(e.g., nitrogenase (flavodoxin)).

The oxidoreductases which act on phosphorus or arsenic in donors caninclude, but are not limited to, those with NAD(P)⁺ as acceptor (e.g.phosphonate dehydrogenase), with a cytochrome as acceptor (e.g.,arsenate reductase (cytochrome c)), with disulfide as acceptor (e.g.,arsenate reductase (glutaredoxin), methylarsonate reductase, andmycoredoxin), with a copper protein as acceptor (e.g. arsenate reductase(azurin)), and with other acceptors (e.g. arsenate reductase (donor)).

The oxidoreductases which act on X-H and Y-H to form an X-Y bond caninclude, but are not limited to, those with oxygen as acceptor (e.g.,isopenicillin-N synthase, columbamine oxidase, reticuline oxidase,sulochrin oxidase [(+)-bisdechlorogeodin-forming], sulochrin oxidase[(−)-bisdechlorogeodin-forming], and aureusidin synthase), with adisulfide as acceptor (e.g., D-proline reductase (dithiol), glycinereductase, sarcosine reductase, and betaine reductase), and with otheracceptors (e.g., β-cyclopiazonate dehydrogenase).

The oxidoreductases which act on halogen in donors can include, but arenot limited to, those with NAD or NADP as acceptor (e.g. iodotyrosinedeiodinase).

Other oxidoreductases can include, but are not limited to, chloratereductase, pyrogallol hydroxyltransferase, sulfur reductase,[formate-C-acetyltransferase]activating enzyme, tetrachloroethenereductive dehalogenase, selenate reductase, thyroxine 5′-deiodinase,thyroxine 5-deiodinase, and photosystem I).

Suitable oxidoreductases include various sugar oxidases, laccases,peroxidases and haloperoxidases.

Glycosylases

Glycosylases include glycosidases, i.e. enzymes hydrolyzing O- andS-glycosyl compounds, including but not limited to a-amylase,(3-amylase, glucan 1,4-α-glucosidase, cellulase,endo-1,3(4)-β-glucanase, inulinase, endo-1,4-β-xylanase,oligo-1,6-glucosidase, dextranase, chitinase, polygalacturonase,lysozyme, exo-α-sialidase, α-glucosidase, (3-glucosidase,α-galactosidase, β(3-galactosidase, α-mannosidase, β-mannosidase,(3-fructofuranosidase, α,α-trehalase, β-glucuronidase,endo-1,3-β-xylanase, amylo-1,6-glucosidase, hyaluronoglucosaminidase,hyaluronoglucuronidase, xylan 1,4-β-xylosidase, β-D-fucosidase, glucanendo-1,3-β-D-glucosidase, α-L-rhamnosidase, pullulanase,GDP-glucosidase, β-L-rhamnosidase, fucoidanase, glucosylceramidase,galactosylceramidase, galactosylgalactosylglucosylceramidase, sucroseα-glucosidase, α-N-acetylgalactosaminidase, α-N-acetylglucosaminidase,α-L-fucosidase, β-L-N-acetylhexosaminidase, β-N-acetylgalactosaminidase,cyclomaltodextrinase, α-N-arabinofuranosidase,glucuronosyl-disulfoglucosamine glucuronidase, isopullulanase, glucan1,3-β-glucosidase, glucan endo-1,3-α-glucosidase, glucan1,4-α-maltotetraohydrolase, mycodextranase, glycosylceramidase,1,2-α-L-fucosidase, 2,6-(3-fructan 6-levanbiohydrolase, levanase,quercitrinase, galacturan 1,4-α-galacturonidase, isoamylase, glucan1,6-α-glucosidase, glucan endo-1,2-β-glucosidase, xylan1,3-β-xylosidase, licheninase, glucan 1,4-β-glucosidase, glucanendo-1,6-β-glucosidase, L-iduronidase, mannan 1,2-(1,3)-α-mannosidase,mannan endo-1,4-β-mannosidase, fructan β-fructosidase, β-agarase,exo-poly-α-galacturonosidase, κ-carrageenase, glucan 1,3-α-glucosidase,6-phospho-3-galactosidase, 6-phospho-β-glucosidase,capsular-polysaccharide endo-1,3-α-galactosidase, β-L-arabinosidase,arabinogalactan endo-1,4-β-galactosidase, cellulose 1,4-β-cellobiosidase(non-reducing end), peptidoglycan β-N-acetylmuramidase,α,α-phosphotrehalase, glucan 1,6-α-isomaltosidase, dextran1,6-α-isomaltotriosidase, mannosyl-glycoproteinendo-3-N-acetylglucosaminidase, endo-α-N-acetylgalactosaminidase, glucan1,4-α-maltohexaosidase, arabinan endo-1,5-α-L-arabinanase, mannan1,4-mannobiosidase, mannan endo-1,6-α-mannosidase, blood-group-substanceendo-1,4-β-galactosidase, keratan-sulfate endo-1,4-β-galactosidase,steryl-β-glucosidase, strictosidine β-glucosidase,mannosyl-oligosaccharide glucosidase,protein-glucosylgalactosylhydroxylysine glucosidase, lactase,endogalactosaminidase, 1,3-α-L-fucosidase, 2-deoxyglucosidase,mannosyl-oligosaccharide 1,2-α-mannosidase, mannosyl-oligosaccharide1,3-1,6-α-mannosidase, branched-dextran exo-1,2-α-glucosidase, glucan1,4-α-maltotriohydrolase, amygdalin β-glucosidase, prunasinβ-glucosidase, vicianin β-glucosidase, oligoxyloglucan β-glycosidase,polymannuronate hydrolase, maltose-6′-phosphate glucosidase,endoglycosylceramidase, 3-deoxy-2-octulosonidase, raucaffricineβ-glucosidase, coniferin β-glucosidase, 1,6-α-L-fucosidase,glycyrrhizinate β-glucuronidase, endo-α-sialidase, glycoproteinendo-α-1,2-mannosidase, xylan α-1,2-glucuronosidase, chitosanase, glucan1,4-α-maltohydrolase, difructose-anhydride synthase, neopullulanase,glucuronoarabinoxylan endo-1,4-β-xylanase, mannanexo-1,2-1,6-α-mannosidase, α-glucuronidase, lacto-N-biosidase,4-α-D-{(1→4)-α-D-glucano}trehalose trehalohydrolase, limit dextrinase,poly(ADP-ribose) glycohydrolase, 3-deoxyoctulosonase, galactan1,3-β-galactosidase, β-galactofuranosidase, thioglucosidase,β-primeverosidase, oligoxyloglucan reducing-end-specificcellobiohydrolase, xyloglucan-specific endo-β-1,4-glucanase,mannosylglycoprotein endo-β-mannosidase, fructan β-(2,1)-fructosidase,fructan β-(2,6)-fructosidase, xyloglucan-specific exo-β-1,4-glucanase,oligosaccharide reducing-end xylanase, t-carrageenase, a-agarase,a-neoagaro-oligosaccharide hydrolase, β-apiosyl-β-glucosidase,k-carrageenase, 1,6-α-D-mannosidase, galactan endo-1,6-β-galactosidase,exo-1,4-β-D-glucosaminidase, heparanase, baicalin-β-D-glucuronidase,hesperidin 6-O-α-L-rhamnosyl-β-D-glucosidase, protein O-GlcNAcase,mannosylglycerate hydrolase, rhamnogalacturonan hydrolase, unsaturatedrhamnogalacturonyl hydrolase, rhamnogalacturonan galacturonohydrolase,rhamnogalacturonan rhamnohydrolase, β-D-glucopyranosyl abscisateβ-glucosidase, cellulose 1,4-β-cellobiosidase (reducing end),α-D-xyloside xylohydrolase, and β-porphyranase.

Glycosylases also include hydrolyzing N-glycosyl compounds, includingbut not limited to purine nucleosidase, inosine nucleosidase, uridinenucleosidase, AMP nucleosidase, NAD+nucleosidase, NAD(P)⁺ nucleosidase,adenosine nucleosidase, ribosylpyrimidine nucleosidase,adenosylhomocysteine nucleosidase, pyrimidine-5′-nucleotidenucleosidase, β-aspartyl-N-acetylglucosaminidase, inosinatenucleosidase, 1-methyladenosine nucleosidase, NMN nucleosidase,DNA-deoxyinosine glycosylase, methylthioadenosine nucleosidase,deoxyribodipyrimidine endonucleosidase, ADP-ribosylarginine hydrolase,DNA-3-methyladenine glycosylase I, DNA-3-methyladenine glycosylase II,rRNA N-glycosylase, DNA-formamidopyrimidine glycosylase,ADP-ribosyl-[dinitrogen reductase] hydrolase, N-methyl nucleosidase,futalosine hydrolase, uracil-DNA glycosylase, double-stranded uracil-DNAglycosylase, and thymine-DNA glycosylase, and hydrolyzing S-glycosylcompounds.

Hydrolases

Hydrolases of EC 3 include, but are not limited to: those acting onester bonds; glycosylases, those acting on ether bonds; those acting onpeptide bonds (peptidases/proteases); those acting on carbon-nitrogenbonds, other than peptide bonds; those acting on acid anhydrides; thoseacting on carbon-carbon bonds; those acting on halide bonds; thoseacting on phosphorus-nitrogen bonds; those acting on sulfur-nitrogenbonds; those acting on carbon-phosphorus bonds; those acting onsulfur-sulfur bonds; and those acting on carbon-sulfur bonds.

The hydrolases of EC 3 which act on ester bonds, can include, but arenot limited to, carboxylic ester hydrolases (for example lipasesincluding triacylglycerol lipase, phospholipase A₁, phospholipase A₂,lysophospholipase, acylglycerol lipase, galactolipase, lipoproteinlipase; and phosphoric diester hydrolases including phosphlipase C,phospholipase D, phosphoinositide phospholipase C,glycosylphosphatidylinositol phospholipase D, andN-acetylphosphatidylethanolamine-hydrolysing phospholipase D) andglycosylases, including glycosidases, i.e. enzymes hydrolysing O- andS-glycosyl compounds, for example amylases (including alpha-amylase,beta-amylase, and isoamylase), cellulases, and mannanases.

Suitable lipases and cutinases include those of bacterial or fungalorigin. Chemically modified or protein engineered mutants are included.Examples include lipase from Thermomyces, e.g., from T. lanuginosus(previously named Humicola lanuginosa) as described in EP 258 068 (andU.S. Pat. No. 4,810,414) and EP 305 216 (and U.S. Pat. Nos. 5,766,912;5,874,558; 5,965,384; 7,517,668; 5,536,661 and 5,863,759), cutinase fromHumicola, e.g. H. insolens as described in WO 96/13580, a Pseudomonaslipase, e.g., from P. alcaligenes or P. pseudoalcaligenes (EP 218 272,U.S. Pat. Nos. 5,766,912; 5,863,759; 5,874,558; 5,965,384; 7,517,668 and5,536,661), P. cepacia (EP 331 376 and U.S. Pat. No. 5,290,694), P.stutzeri (GB 1,372,034), P. fluorescens, Pseudomonas sp. strain SD 705(WO 95/06720, U.S. Pat. No. 5,827,718, WO 96/27002, and U.S. Pat. No.5,942,431), P. wisconsinensis (WO 96/12012), a Bacillus lipase, e.g.,from B. subtilis (Dartois et al., 1993, Biochemica et Biophysica Acta,1131: 253-360), B. stearothermophilus (JP 64/744992) or B. pumilus (WO91/16422 and U.S. Pat. No. 5,427,936). Other examples are lipasevariants such as those described in WO 92/05249, WO 94/01541, EP 407225, EP 260 105, WO 95/35381, WO 96/00292, WO 95/30744, WO 94/25578, WO95/14783, WO 95/22615, WO 97/04079, WO 97/07202, WO 00/060063,WO2007/087508, WO 2009/109500 and U.S. Pat. Nos. 5,892,013; 5,869,438;5,976,855; 6,020,180; 6,074,863; 5,658,871; 4,760,025; 5,155,033;5,182,204; 5,185,258; 5,204,015; 5,244,791; 5,264,366; 5,310,675;5,316,941; 5,346,823; 5,352,594; 5,371,008; 5,371,190; 5,411,873;5,441,882; 5,472,855; 5,652,136; 5,700,676; 5,763,257; 5,801,038;5,939,315; 5,955,340; 5,972,682; 6,465,235; and RE34,606. Preferredcommercially available lipase enzymes include Lipolase™, LipolaseUltra™, and Lipex™; Lecitase™, Lipolex™; Lipoclean™, Lipoprime™(Novozymes A/S). Other commercially available lipases include Lumafast(Genencor Int Inc); Lipomax, M1 Lipase (Gist-Brocades/Genencor Int Inc),and Bacillus sp lipase from Solvay.

Suitable amylases (α and/or β) include those of bacterial or fungalorigin. Chemically modified or protein engineered mutants are included.Amylases include, for example, α-amylases obtained from Bacillus, e.g.,a special strain of Bacillus licheniformis, described in more detail inGB 1,296,839. Examples of useful amylases are the variants described inWO 94/02597, WO 94/18314, WO 96/23873, WO 97/43424, U.S. Pat. Nos.5,824,532; 5,849,549; 6,297,037; 6,093,562; 6,297,038; 6,867,031; andU.S. Publication Nos. 2002/0098996; 2003/0064908; 2004/0253676;2005/0059131; 2005/0250664; 2006/0035323; 2009/0280527; 2010/0099597;2010/0099598; and 2011/0177990, especially the variants withsubstitutions in one or more of the following positions: 15, 23, 105,106, 124, 128, 133, 154, 156, 181, 188, 190, 197, 202, 208, 209, 243,264, 304, 305, 391, 408, and 444. Commercially available amylases areDuramyl™, Termamyl™, Fungamyl™, Natalase™ and BAN™ (Novozymes A/S),Rapidase™ and Purastar™ (from Genencor International Inc.).

Suitable cellulases include those of bacterial or fungal origin.Chemically modified or protein engineered mutants are included. Suitablecellulases include cellulases from the genera Bacillus, Pseudomonas,Humicola, Fusarium, Thielavia, Acremonium, e.g., the fungal cellulasesproduced from Humicola insolens, Myceliophthora thermophila and Fusariumoxysporum disclosed in U.S. Pat. Nos. 4,435,307; 5,648,263; 5,691,178;5,776,757 and WO 89/09259. Especially suitable cellulases are thealkaline or neutral cellulases having color care benefits. Examples ofsuch cellulases are cellulases described in EP 0 495 257, EP 0 531 372,WO 96/11262, WO 96/29397, WO 98/08940, U.S. Pat. Nos. 5,520,838;5,443,750; 5,668,073; 5,948,672; 6,423,524; 5,919,691; 6,071,735;6,001,639; 6,387,690; 6,855,531; 7,226,773; and U.S. Publication Nos.2001/0036910; 2003/0119167; 2003/0054539; 2005/0070003; 2008/0145912;and 2010/0107342. Other examples are cellulase variants such as thosedescribed in WO 94/07998, EP 0 531 315, WO 95/24471, WO 98/12307,PCT/DK98/00299, U.S. Pat. Nos. 5,457,046; 5,686,593; 5,763,254;5,792,641; 6,114,296; 5,457,046; 5,912,157; 6,117,664; 7,993,898;8,017,372; and U.S. Publication Nos. 2003/0092097; 2005/0009166;2008/0206836; 2009/0170747 and 2011/0250674. Commercially availablecellulases include Celluzyme™, and Carezyme™ (Novozymes A/S),Clazinase™, and Puradax HA™ (Genencor International Inc.), andKAC-500(B)™ (Kao Corporation).

Peptidases/Proteases

The hydrolases of EC 3 which act on peptide bonds (peptidases/proteases)can include, but are not limited to aminopeptidases (including leucylaminopeptidase, membrane alanyl aminopeptidase, cystinyl aminopeptidase,tripeptide aminopeptidase, prolyl aminopeptidase, arginylaminopeptidase, glutamyl aminopeptidase, Xaa-Pro aminopeptidase,bacterial leucyl aminopeptidase, clostridial aminopeptidase, cytosolalanyl aminopeptidase, lysyl aminopeptidase, Xaa-Trp aminopeptidase,tryptophanyl aminopeptidase, methionyl aminopeptidase, D-stereospecificaminopeptidase, aminopeptidase Ey, aspartyl aminopeptidase,aminopeptidase I, PepB aminopeptidase, aminopeptidase S, beta-peptidylaminopeptidase, and intermediate cleaving peptidase 55); dipeptidases(including Xaa-Arg dipeptidase. Xaa-methyl-His dipeptidase, Glu-Gludipeptidase, Xaa-Pro dipeptidase, Met-Xaa dipeptidase,non-stereospecific dipeptidase, cytosol nonspecific dipeptidase,membrane dipeptidase, beta-Ala-His dipeptidase, dipeptidase E, andD-Ala-D-Ala dipeptidase); Dipeptidyl-peptidases andtripeptidyl-peptidases (including dipeptidyl-peptidase I,dipeptidyl-peptidase II, dipeptidyl-peptidase III, dipeptidyl-peptidaseIV, dipeptidyl-dipeptidase, tripeptidyl-peptidase I,tripeptidyl-peptidase II, Xaa-Pro dipeptidyl-peptidase, andprolyltripeptidyl aminopeptidase); peptidyl-dipeptidases (includingpeptidyl-dipeptidase A, peptidyl-dipeptidase B, peptidyl-dipeptidaseDcp, and cyanophycinase); serine-type carboxypeptidases (includinglysosomal Pro-Xaa carboxypeptidase, serine-type D-Ala-D-Alacarboxypeptidase, carboxypeptidase C, and carboxypeptidase D);metallocarboxypeptidases (including carboxypeptidase A, carboxypeptidaseB, lysine carboxypeptidase, Gly-Xaa carboxypeptidase, alaninecarboxypeptidase, muramoylpentapeptide carboxypeptidase,carboxypeptidase E, glutamate carboxypeptidase, carboxypeptidase M,muramoyltetrapeptide carboxypeptidase, zinc D-Ala-D-Alacarboxypeptidase, carboxypeptidase A2, membrane Pro-Xaacarboxypeptidase, tubulinyl-Tyr carboxypeptidase, carboxypeptidase T,carboxypeptidase Taq, carboxypeptidase U, glutamate carboxypeptidase II,metallocarboxypeptidase D, and angiotensin-converting enzyme 2);ccysteine-type carboxypeptidases, including cathepsin X; omegapeptidases (including acylaminoacyl-peptidase, peptidyl-glycinamidase,pyroglutamyl-peptidase I, beta-aspartyl-peptidase,pyroglutamyl-peptidase II, N-formylmethionyl-peptidase, gamma-glutamylhydrolase, gamma-D-glutamyl-meso-diaminopimelate peptidase I, andubiquitinyl hydrolase 1); serine endopeptidases (including chymotrypsin,chymotrypsin C, metridin, trypsin, thrombin, coagulation factor Xa,plasmin, enteropeptidase, acrosin, alpha-Lytic endopeptidase, glutamylendopeptidase, cathepsin G, coagulation factor VIIa, coagulation factorIXa, cucumisin, prolyl oligopeptidase, coagulation factor XIa,brachyuran, plasma kallikrein, tissue kallikrein, pancreatic elastase,leukocyte elastase, coagulation factor XIIa, chymase, complementsubcomponent C ^(1r) , complement subcomponent C ^(1s) ,classical-complement-pathway C3/C5 convertase, complement factor I,complement factor D, alternative-complement-pathway C3/C5 convertase,cerevisin, hypodermin C, lysyl endopeptidase, endopeptidase La,gamma-renin, venombin AB, leucyl endopeptidase, tryptase, scutelarin,kexin, subtilisin, oryzin, peptidase K, thermomycolin, thermitase,endopeptidase So, t-plasminogen activator, protein C (activated),pancreatic endopeptidase E, pancreatic elastase II, IgA-specific serineendopeptidase, u-plasminogen activator, venombin A, furin, myeloblastin,semenogelase, granzyme A, granzyme B, streptogrisin A, streptogrisin B,glutamyl endopeptidase II oligopeptidase B, limulus clotting factor C,limulus clotting factor B, limulus clotting enzyme, repressor LexA,signal peptidase I, togavirin, flavivirin, endopeptidase Clp, proproteinconvertase 1, proprotein convertase 2, snake venom factor V activator,lactocepin, assembling, hepacivirin, spermosin, sedolisin,xanthomonalisin, C-terminal processing peptidase, physarolisin,mannan-binding lectin-associated serine protease-2, rhomboid protease,hepsin, peptidase Do, HtrA2 peptidase, matriptase, C5a peptidase,aqualysin 1, site-1 protease, pestivirus NS3 polyprotein peptidase,equine arterivirus serine peptidase, infectious pancreatic necrosisbirnavirus Vp4 peptidase, SpoIVB peptidase, stratum corneum chymotrypticenzyme, kallikrein 8, kallikrein 13, and oviductin); cysteineendopeptidases(including cathepsin B, papain, ficain, chymopapain,asclepain, clostripain, streptopain, actinidain, cathepsin L, cathepsinH, cathepsin T, glycyl endopeptidase, cancer procoagulant, cathepsin S,picornain 3C, picornain 2A, caricain, ananain, stem bromelain, fruitbromelain, legumain, histolysain, caspase-1, gingipain R, cathepsin K,adenain, bleomycin hydrolase, cathepsin F, cathepsin V, cathepsin O,nuclear-inclusion-a endopeptidase, helper-component proteinase,L-peptidase, gingipain K, staphopain, separase, V-cath endopeptidase,cruzipain, calpain-1, calpain-2, calpain-3, caspase-2, caspase-3,caspase-4, caspase-5, caspase-6, caspase-7, caspase-8, caspase-9,caspase-10, caspase-11, peptidase 1 (mite), calicivirin, zingipain, Ulp1peptidase, SARS coronavirus main proteinase, sortase A, and sortase B);aspartic endopeptidases (including pepsin A, pepsin B, gastricsin,chymosin, cathepsin D, nepenthesin, renin, HIV-1 retropepsin,Pro-opiomelanocortin converting enzyme, aspergillopepsin I,aspergillopepsin II, penicillopepsin, rhizopuspepsin, endothiapepsin,mucorpepsin, candidapepsin, saccharopepsin, rhodotorulapepsin,acrocylindropepsin, polyporopepsin, pycnoporopepsin, scytalidopepsin A,scytalidopepsin B, cathepsin E, barrierpepsin, signal peptidase II,plasmepsin I, plasmepsin II, phytepsin, yapsin 1, thermopsin, prepilinpeptidase, nodavirus endopeptidase, memapsin 1, memapsin 2, HIV-2retropepsin, plasminogen activator Pla, omptin, human endogenousretrovirus K endopeptidase, and HycI peptidase); metalloendopeptidases(including atrolysin A, microbial collagenase, leucolysin, interstitialcollagenase, neprilysin, envelysin, IgA-specific metalloendopeptidase,procollagen N-endopeptidase, thimet oligopeptidase, neurolysin,stromelysin 1, meprin A, procollagen C-endopeptidase, peptidyl-Lysmetalloendopeptidase, astacin, stromelysin 2, matrilysin, gelatinase A,vibriolysin, pseudolysin, thermolysis, bacillolysin, aureolysin,coccolysin, mycolysin, β-lytic metalloendopeptidase, peptidyl-Aspmetalloendopeptidase, neutrophil collagenase, gelatinase B,leishmanolysin, saccharolysin, gametolysin, deuterolysin, serralysin,atrolysin B, atrolysin C, atroxase, atrolysin E, atrolysin F,adamalysin, horrilysin, ruberlysin, bothropasin, bothrolysin,ophiolysin, trimerelysin I, trimerelysin II, mucrolysin, pitrilysin,insulysin, O-sialoglycoprotein endopeptidase, russellysin, mitochondrialintermediate peptidase, dactylysin, nardilysin, magnolysin, meprin B,mitochondrial processing peptidase, macrophage elastase, choriolysin L,choriolysin H, tentoxilysin, bontoxilysin, oligopeptidase A,endothelin-converting enzyme, fibrolase, jararhagin, fragilysin,lysostaphin, flavastacin, snapalysin, gpr endopeptidase, pappalysin-1,membrane-type matrix metalloproteinase-1, ADAM10 endopeptidase, ADAMTS-4endopeptidase, anthrax lethal factor endopeptidase, Ste24 endopeptidase,S2P endopeptidase, ADAM 17 endopeptidase, and ADAMTS13 endopeptidase);and threonine endopeptidases (including proteasome endopeptidase complexand HslU-HslV peptidase).

Suitable proteases include those of animal, vegetable or microbialorigin. Microbial origin is preferred. Chemically modified or proteinengineered mutants are included. The protease may be a serine proteaseor a metalloprotease, preferably an alkaline microbial protease or atrypsin-like protease. Examples of alkaline proteases are subtilisins,especially those derived from Bacillus, e.g., subtilisin Novo,subtilisin Carlsberg, subtilisin 309, subtilisin 147 and subtilisin 168(described in WO 89/06279, U.S. Pat. Nos. 6,506,589; 6,808,913;6,835,821; and U.S. Publication Nos. 2003/0148495; 2003/0175933;2003/0186378 and 2005/0003986). Examples of trypsin-like proteases aretrypsin (e.g., of porcine or bovine origin) and the Fusarium proteasedescribed in WO 89/06270, WO 94/25583, and U.S. Pat. Nos. 5,288,627 and5,693,520. Examples of useful proteases are the variants described in WO92/19729, WO 98/20115, WO 98/20116, WO 98/34946, and U.S. Pat. Nos.5,858,757; 6,300,116; 7,098,017; 6,159,731; and US Publication No.2002/0102702, especially the variants with substitutions in one or moreof the following positions: 27, 36, 57, 76, 87, 97, 101, 104, 120, 123,167, 170, 194, 206, 218, 222, 224, 235, and 274. Preferred commerciallyavailable protease enzymes include Alcalase™, Savinase™, Primase™,Duralase™, Esperase™, and Kannase™ (Novozymes A/S), Maxatase™, Maxacal™,Maxapem™, Properase™, Purafect™ Purafect OxP™, FN2™, and FN3™ (GenencorInternational Inc.)

Enzymes for use in laundry and dishwashing applications can include oneor more of protease, amylase, lipase, dehydrogenase, transaminase,kinase, cellulase, mannanase, peptidase, decarboxylase, isomerase,mutase, synthetase, synthase, and oxido-reductase enzymes, includingoxido-reductase enzymes that catalyze the formation of bleaching agents.

It is contemplated that an enzyme for use in a powder described hereincan come from any suitable source or combination of sources, for examplebacterial, fungal, plant, or animal sources. In one type of embodiment,a mixture of two or more enzymes will come from at least two differenttypes of sources. For example, a mixture of protease and lipase can comefrom a bacterial (protease) and fungal (lipase) sources.

Optionally, an enzyme for use herein, including but not limited to anyenzyme class or member described herein, is one which works in alkalinepH conditions, e.g. for use in detergent applications including laundrydetergent and/or dish detergent, e.g. a pH in a range of about 8 toabout 11. Optionally, an enzyme for use herein, including but notlimited to any enzyme class or member described herein, is one whichworks in a temperature in a range of about 5° C. to about 45° C.

Oils other than fragrances can include flavorants and colorants.

In one class of embodiments the active agent comprises a flavor orcombination of flavors. Suitable flavors include but are not limited to,spearmint oil, cinnamon oil, oil of wintergreen (methylsalicylate),peppermint oils, and synthetic and natural fruit flavors, includingcitrus oils.

In some embodiments, the active agent may be a colorant or combinationof colorants. Examples of suitable colorants include food colorings,caramel, paprika, cinnamon, and saffron. Other examples of suitablecolorants can be found in U.S. Pat. No. 5,002,789, hereby incorporatedby reference in its entirety.

Another class of embodiments include one or more odor absorbers asactive agents. Suitable odor absorbers for use as active agentsaccording to the disclosure include, but are not limited to, zeolites,and complex zinc salts of ricinoleic acid. The odor absorbing activeagent can also comprise fixatives that are well known in the art aslargely odor-neutral fragrances, including but not limited to extractsof labdanum, styrax, and derivatives of abietic acid.

Another class of embodiments include one or more fragrances as activeagents. As used herein, the term fragrance refers to any applicablematerial that is sufficiently volatile to produce a scent. Embodimentsincluding fragrances as active agents can include fragrances that arescents pleasurable to humans, or alternatively fragrances that arescents repellant to humans, animals, and/or insects. Suitable fragrancesinclude, but are not limited to, fruits including, but not limited to,lemon, apple, cherry, grape, pear, pineapple, orange, strawberry,raspberry, musk and flower scents including, but not limited to,lavender-like, rose-like, iris-like and carnation-like. Optionally thefragrance is one which is not also a flavoring. Other fragrances includeherbal scents including, but not limited to, rosemary, thyme, and sage;and woodland scents derived from pine, spruce and other forest smells.Fragrances may also be derived from various oils, including, but notlimited to, essential oils, or from plant materials including, but notlimited to, peppermint, spearmint and the like. Suitable fragrant oilscan be found in U.S. Pat. No. 6,458,754, hereby incorporated byreference in its entirety. Suitable fragrant oils include, but are notlimited to, 4-(2,2,6-trimethylcyclohex-1-enyl)-2-en-4-one, acetaldehydephenyletheyl propyl acetal, 2,6,10-trimethyl-9-undecenal, hexanoic acid2-propenyl ester, 1-octen-3-ol, trans-anethole, iso buthyl(z)-2-methyl-2-butenoate, anisaldehyde diethyl acetal,3-methyl-5-propyl-cyclohezen-1-one,2,4-dimethyl-3-cyclohexene-1-carbaldehyde, trans-4-decenal, decanal,2-pentylcyclopentanone, ethyl anthranilate, eugenol,3-(3-isopropylphenyl)butanoal, methyl 2-octynoate, isoeugenol,cis-3-hexenyl methyl carbonate, linalool, methyl-2-nonynonate, benzoicacid 2-hydroxymethyl ester, nonal, octanal, 2-nonennitrile,4-nonanolide, 9-decen-l-ol, and 10-undecen-1-al. Applicable fragrancescan also be found in U.S. Pat. Nos. 4,534,981, 5,112,688, 5,145,842,6,844,302 and Perfumes Cosmetics and Soaps, Second Edition, edited by W.A. Poucher, 1959, all hereby incorporated by reference in theirentireties. These fragrances include acacia, cassie, chypre, cyclamen,fern, gardenia, hawthorn, heliotrope, honeysuckle, hyacinth, jasmine,lilac, lily, magnolia, mimosa, narcissus, freshly-cut hay, orangeblossom, orchids, reseda, sweet pea, trefle, tuberose, vanilla, violet,wallflower, and the like.

Applicable insect repellant fragrances include one or more ofdichlorvos, pyrethrin, allethrin, naled and/or fenthion pesticidesdisclosed in U.S. Pat. No. 4,664,064, incorporated herein by referencein its entirety. Suitable insect repellants are citronellal(3,7-dimethyl-6-octanal), N,N-diethyl-3-methylbenzamide (DEET),vanillin, and the volatile oils extracted from turmeric (Curcuma longa),kaffir lime (Citrus hystrix), citronella grass (Cymbopogon winterianus)and hairy basil (Ocimum americanum). Moreover, applicable insectrepellants can be mixtures of insect repellants.

In one class of embodiments, the active agents according to thedisclosure can comprise one or more pesticides. Suitable pesticides mayinclude, but are not limited to, insecticides, herbicides, acaricides,fungicides, and larvacides.

Another class of embodiments include one or more fertilizers as activeagents. As used herein, the term fertilizer applies to any applicablematerial that releases one or more of nitrogen, phosphorus, potassium,calcium, magnesium, sulfur, boron, chlorine, copper, iron, manganese,molybdenum, or zinc. Suitable fertilizers include, but are not limitedto zeolites. For example, clinoptilolite is a zeolite that releasespotassium and can also release nitrogen when preloaded with ammonium.

One class of embodiments comprise acid catalysts as active agents. Asused herein, the term acid catalysts refers to any species that servesas a proton source, thereby facilitating a chemical reaction. In onetype of embodiment, the acid catalyst will be a non-oxidizing organicacid. A suitable organic acid is para-toluenesulfonic acid. In someembodiments, active agents that are acid catalysts will facilitatereactions including, but not limited to, acetalization, esterificationor transesterification. Additional acid catalyzed reactions are wellknown in the art.

In one class of embodiments, active agents will include metal catalysts.These catalysts mediate reactions including, but not limited to,oxidation or reduction, hydrogenation, carbonylation, C—H bondactivation, and bleaching. Suitable metals for use as metal catalystsinclude, but are not limited to the VIIIA and IB transition metals, forexample, iron, cobalt, nickel, copper, platinum, rhodium, ruthenium,silver, osmium, gold and iridium. The metal that mediates catalysis canbe of any suitable oxidation state.

In alternative embodiments, the active agent may optionally be an ionscavenger. Suitable ion scavengers include, but are not limited to,zeolites. Optionally, zeolites can be added to water-soluble packetscomprising laundry detergents or dish washing detergents enclosedwithin, as a water softener.

Inorganic and organic bleaches are suitable cleaning active agents foruse herein. Inorganic bleaches include perhydrate salts including, butnot limited to, perborate, percarbonate, perphosphate, persulfate andpersilicate salts. The inorganic perhydrate salts are normally thealkali metal salts. Alkali metal percarbonates, particularly sodiumpercarbonate are suitable perhydrates for use herein. Organic bleachescan include organic peroxyacids including diacyl and tetraacylperoxides,especially, but not limited to, diperoxydodecanedioc acid,diperoxytetradecanedioc acid, and diperoxyhexadecanedioc acid. Dibenzoylperoxide is a suitable organic peroxyacid according to the disclosure.Other organic bleaches include the peroxy acids, particular examplesbeing the alkylperoxy acids and the arylperoxy acids.

In one class of embodiments, active agents can comprise bleachactivators, including organic peracid precursors that enhance thebleaching action in the course of cleaning at temperatures of 60° C. andbelow. Bleach activators suitable for use herein include compoundswhich, under perhydrolysis conditions, give aliphatic peroxoycarboxylicacids having from 1 to 10 carbon atoms, or from 2 to 4 carbon atoms,and/or optionally substituted perbenzoic acid. Suitable substances bearO-acyl and/or N-acyl groups of the number of carbon atoms specifiedand/or optionally substituted benzoyl groups. Suitable substancesinclude, but are not limited to, polyacylated alkylenediamines, inparticular tetraacetylethylenediamine (TAED), acylated triazinederivatives, in particular1,5-diacetyl-2,4-dioxohexahydro-1,3,5-triazine (DADHT), acylatedglycolurils, in particular tetraacetylglycoluril (TAGU), N-acylimides,in particular N-nonanoylsuccinimide (NOSI), acylated phenolsulfonates,in particular n-nonanoyl- or isononanoyloxybenzenesulfonate (n- oriso-NOBS), carboxylic anhydrides, in particular phthalic anhydride,acylated polyhydric alcohols, in particular triacetin, ethylene glycoldiacetate and 2,5-diacetoxy-2,5-dihydrofuran and also triethylacetylcitrate (TEAC).

In embodiments that comprise fabric softeners as active agents, variousthrough-the-wash fabric softeners, especially the impalpable smectiteclays of U.S. Pat. No. 4,062,647, incorporated herein by reference inits entirety, as well as other softener clays known in the art, canoptionally be used to provide fabric softener benefits concurrently withfabric cleaning. Clay softeners can be used in combination with amineand cationic softeners as disclosed, for example, in U.S. Pat. Nos.4,375,416 and 4,291,071, incorporated herein by reference in theirentireties.

Active agents may be solids or liquids. Active agents that are solidscan have an average particle size of at least about 0.01 μm, or a sizein a range of about 0.01 μm to about 2 mm, for example. Liquid activeagents may be mixed with a carrier powder directly or microencapsulated.In embodiments that comprise a carrier powder, the average particle sizeof the carrier powder can be at least about 0.01 μm, or in a range ofabout 0.01 μm to about 2 mm, for example. In embodiments that comprisethe microencapsulation of the active agent, the particle size of thesolid active agent or carrier powder, that has active agent adsorbed,need only be sufficiently small enough to enable it to bemicroencapsulated. In coating powders according to the disclosure, theactive agent can be present in the coating powder in an amount of atleast about 1 wt %, or in a range of about 1 wt % to about 99 wt %.

In one class of embodiments the active agent is encapsulated, allowingfor the controlled release of the active agent. Suitable microcapsulescan include or be made from one or more of melamine formaldehyde,polyurethane, urea formaldehyde, chitosan, polymethyl methacrylate,polystyrene, polysulfone, poly tetrahydrofuran, gelatin, gum arabic,starch, polyvinyl pyrrolidone, carboxymethylcellulose,hydroxyethylcellulose, methylcellulose, arabinogalactan, polyvinylalcohol, polyacrylic acid, ethylcellulose, polyethylene,polymethacrylate, polyamide, poly (ethylenevinyl acetate), cellulosenitrate, silicones, poly(lactideco-glycolide), paraffin, carnauba,spermaceti, beeswax, stearic acid, stearyl alcohol, glyceryl stearates,shellac, cellulose acetate phthalate, zein, and combinations thereof. Inone type of embodiment, the microcapsule is characterized by a meanparticle size of at least about 0.1 micron, or in a range of about 0.1micron to about 200 microns, for example. In alternate embodiments, themicrocapsules can form agglomerates of individual particles, for examplewherein the individual particles have a mean particle size of at leastabout 0.1 micron, or in a range of about 0.1 micron to about 200microns.

Examples of microcapsules that may form agglomerates include, but arenot limited to, melamine formaldehyde, polyurethane, urea formaldehyde,chitosan, polymethyl methacrylate, polystyrene, polysulfone,polytetrahydrofuran, gelatin, gum arabic, starch, polyvinyl pyrrolidone,carboxymethylcellulose, hydroxyethylcellulose, methylcellulose,arabinogalactan, polyvinyl alcohol, polyacrylic acid, ethylcellulose,polyethylene, polymethacrylate, polyamide, poly(ethylenevinyl acetate),cellulose nitrate, silicones, poly(lactidoco-glycolide), paraffin,carnauba, spermaceti, beeswax, stearic acid, stearyl alcohol, glycerylstearates, shellac, cellulose acetate phthalate, and zein.

Mechanisms for the controlled release of the active agent from themicrocapsule can include one or more of mechanical rupture, dissolution,diffusion release, ablation release, biodegradation, melting, andpH-triggered release. In embodiments wherein a mechanical rupturerelease mechanism is employed, the mean particle size of themicrocapsule particle or agglomerate can be greater than the meanparticle size of the powdered lubricant, for example. Microcapsulessuitable for use in a mechanical rupture mechanism can include one ormore of the group including, but not limited to, melamine formaldehyde,polyurethane, urea formaldehyde, polymethyl methacrylate, andpolytetrahydrofuran.

Suitable microcapsules for use in embodiments that include a dissolutionrelease mechanism can include one or more of the group including, butnot limited to, gelatin, gum arabic, starch, malodextrins,polyvinylpyrrolidone, carboxymethylcellulose, hydroxyethylcellulose,methylcellulose, arabinogalactan, polyvinyl alcohol, and polyacrylicacid.

Suitable microcapsules for use in embodiments that include a diffusionrelease mechanism can include one or more of the group including, butnot limited to, aminoplast capsules with disulfide linkages and melamineformaldehyde microcapsules. Examples of aminoplast capsules withdisulfide linkages can be found in U.S. Pat. No. 6,485,736, hereinincorporated by reference in its entirety.

Suitable microcapsules for use in embodiments that include an ablationrelease mechanism can include one or more of the group including, butnot limited to, ethylcellulose, polyethylene, polymethacrylate,polyamide, poly (ethylenevinyl acetate), cellulose nitrate, silicones,and poly (lactideco-glycolide).

Suitable microcapsules for use in embodiments that include abiodegradation release mechanism can include one or more of the groupincluding, but not limited to, mono- and co-polyesters of the lactic,glycolic, and β-hydroxybutyric acids, as well as δ-valerolactone andε-caprolactones. Examples of microcapsules that utilize a biodegradationrelease mechanism can be found in U.S. Pat. No. 5,648,096, hereinincorporated by reference in its entirety.

Suitable microcapsules for use in embodiments that include a meltrelease mechanism can include one or more of the group including, butnot limited to, polystyrene, polysulfone paraffin, carnauba, spermaceti,beeswax, stearic acid, stearyl alcohol, and glyceryl stearates.

Suitable microcapsules for use in embodiments that include apH-triggered release mechanism can include one or more of the groupincluding, but not limited to, shellac, cellulose acetate phthalate,zein, and chitosan. Polymers with pH-triggered dissolution are describedin U.S. Patent Application Publication 2010/0105821-A1, hereinincorporated by reference in its entirety.

The powdered lubricant can be prepared as a master batch. The coatingpowder composition can be prepared by combining a portion of thepowdered lubricant master batch with the active agent to form a daughterbatch of coating powder. This process can be continuous or intermittent.A continuous feed of active agent can be comprised of multiple activeagent compositions added sequentially, for example, to a feed ofpowdered lubricant.

The coating powder composition can be applied to the film or packet byany suitable means. In a one embodiment, one or more stationary powderspray guns are used to direct the powder stream towards the packets,from one or more than one direction, while the packets are transportedthrough the coating zone by means of a belt conveyor. In an alternativeembodiment, the pouch is conveyed through a suspension of the coatingpowder in air. In yet another alternative embodiment the packets aretumble-mixed with the coating powder in a trough-like apparatus. Inanother embodiment, which can be combined with any other embodiment,electrostatic forces are employed to enhance the attraction between thepowder and the packet. This type of process is typically based onnegatively charging the powder particles and directing these chargedparticles to the grounded packets. In other alternative embodiments, thepowder is applied to the packet by a secondary transferring toolincluding, but not limited to rotating brushes which are in contact withthe powder or by powdered gloves which can transfer the powder from acontainer to the packet. In yet another embodiment the powder is appliedby dissolving or suspending the powder in a non-aqueous solvent which isthen atomized and sprayed onto the packet.

In one class of embodiments, the powder is applied to the packet in anaccurate dose. This class of embodiments utilizes closed-system drylubricant application machinery, such as PekuTECH's powder applicator PM700 D. In this process the coating powder, optionally batch-wise orcontinuously, is fed to a feed trough of application machinery. Thepackets are transferred from the output belt of a standard rotary drumpouch machine onto a conveyor belt of the powder application machine,wherein a controlled dosage of the functionalized coating powder isapplied to the packet. The packet is thereafter conveyed to a suitablesecondary packaging process.

In some embodiments, in use the microcapsule will be mechanicallyruptured thereby releasing the active agent. Suitable active agents tobe released via mechanical rupture include, but are not limited to,fragrances, oils, enzymes, odor absorbers, and activators. In oneembodiment, a fragrance will be microencapsulated, providing acontrolled and efficient delivery mechanism. In this embodiment, thepacket will retain the fragrance until the point of use, upon whichhandling by the consumer will mechanically rupture some of themicrocapsules, releasing the fragrance. This embodiment is advantageousin mitigating the inherent “malodor” of the water-soluble film itself,or from a component of the material packaged in the water-soluble film,in the presence of the consumer.

In alternative embodiments, in use the active agent will be releasedfrom the microcapsule by dissolution of the microcapsule. Suitableactive agents to be released upon microcapsule dissolution include, butare not limited to, flavors, colorants, bleaches, bleach components,enzymes, activators, acid catalysts, metal catalysts, and ionscavengers. In one embodiment, the water-soluble packet may be comprisedof edible water-soluble film. The microencapsulation of a flavor activeor other active agent, for example, allows for the use of ingredientsthat are not or might not be compatible with the water-soluble film. Forexample, an ingredient may cause crosslinking or other reactions thatwould adversely affect the film solubility. The encapsulation of theflavor therefore allows for the inclusion of the ingredient. In otherembodiments the encapsulation of both a flavor and a color would allowfor an enhanced flavor experience and an aesthetically pleasing visualappearance. In one type embodiment, an edible, hot water-soluble filmmay contain a plain, uncolored oatmeal composition. In theseembodiments, upon dissolution of the microcapsule, the color and flavorcan be imparted to the plain, uncolored oatmeal composition, forexample, red and strawberry, blue and blueberry, or brown and maple.Applying the color/flavor microcapsules via the coating powder alsoadvantageously streamlines the manufacturing process and makes for amore flexible supply management, allowing the manufacturer tomass-package a single type of composition, i.e., plain oatmeal, in awater-soluble film and add the color/flavor at a later time.

In one class of embodiments, the active agent will be released from themicrocapsule by diffusion. Suitable active agents for use with adiffusion release mechanism include, but are not limited to, pesticidesand fragrances. In one embodiment the water-soluble packet can contain alaundry composition and the coating powder can comprise a perfume. Inthis embodiment, the fragrance will slowly diffuse from the microcapsuleduring storage, advantageous in mitigating the inherent “malodor” of thewater-soluble film itself, or from a component of the material packagedin the water-soluble film, in the presence of the consumer, and willalso release the remaining fragrance on the laundry substrates duringthe wash cycle.

Embodiments may comprise an ablation or erosion mechanism for therelease of active agents from the microcapsules. Suitable active agentsto be released upon ablation of the microcapsules include, but are notlimited to, bleaches, bleach components, and enzymes. In one embodiment,the composition enclosed in the water-soluble packet may comprise apercarbonate bleaching agent and the microencapsulated active agent maycomprise the bleach activator TAED. In this embodiment, upon ablation,the microcapsule will release the TAED, allowing it to react with thepercarbonate, forming an activated bleach.

In alternative embodiments, the active agent will be released uponbiodegradation of the microcapsule. Suitable active agents for use in abiodegradable microcapsule include, but are not limited to, pesticidesand fertilizers. In one embodiment, a water-soluble packet may contain afertilizer or other lawn-care composition. The packet can be dusted witha biodegradable microcapsule containing a pesticide. After application,the microcapsule will biodegrade, releasing the pesticide. In thisembodiment, the consumer can safely use a single dose of pesticidewithout coming in direct contact with the pesticide.

In some embodiments, the microcapsules will release the active agentupon melting. Suitable active agents to be released when themicrocapsule melts include, but are not limited to, fabric softeners. Inone embodiment, the active agent may comprise a fabric softener. Thefabric softener would be delivered to a laundry substrate via awater-soluble packet comprising a detergent enclosed within the packet.During the wash cycle, the microcapsules would disperse onto the laundrysubstrate, however the fabric softener would not be released until thesubstrate was heated to a temperature not encountered in the clotheswasher (e.g. greater than 40° C. or greater than 50° C., or greater than55° C., or greater than 60° C.) but only encountered in the dryer.

In another type of embodiment, the microcapsule will release the activeagent upon dry brittle failure. For example, in one embodiment theactive agent can include a fabric softener. The fabric softener would bedelivered to a laundry substrate via a water-soluble packet comprising adetergent enclosed within the packet. During the wash cycle, themicrocapsules would disperse onto the laundry substrate, however thefabric softener would not be released until the capsules were driedsufficiently to become brittle and crack, thus releasing their contents.For example, the microcapsules can be designed to become brittle at acritical relative humidity significantly below standard householdconditions, e.g. ≦40%, or <40%, or ≦35%, or <35%, or ≦30%, or <30%,or≦25%, or <25%.

Embodiments may comprise pH triggered release of the active agent fromthe microcapsule. Suitable active agents for a pH triggered release mayinclude, but are not limited to, fragrances, oils, enzymes, odorabsorbers, and activators. In one embodiment the composition enclosed inthe water-soluble packet may comprise a laundry detergent compositionand a first enzyme that is unstable in the presence of a protease, andthe active agent may comprise a protease enzyme. The packet, when placedin a washing machine would dissolve, releasing the detergent compositionand the first enzyme. When the washing water pH is adjusted toappropriate levels the microcapsule would release the protease, therebyallowing a full dose of a first enzyme and a protease to reach a stainedsubstrate. In an alternative embodiment, a protease may be enclosedwithin the packet and the active agent may comprise a second enzymeencapsulated in a microcapsule, wherein the protease would be releasedfirst and upon reaching the appropriate pH, the second enzyme would bereleased. In yet another embodiment, the composition enclosed within thepacket may comprise a first enzyme and the active agent may comprise asecond enzyme, wherein both the first and second enzyme are unstable inthe presence of the other. In another embodiment, the packet can containan automatic dishwasher detergent and the microcapsule can contain arinse aid, wherein the microcapsule is insoluble in highly alkalinesolutions (e.g., pH greater than 9.3, or greater than 10) and soluble inneutral to mildly alkaline conditions, such that the rinse aid is notreleased during the wash cycle but only in the rinse cycle.

The foregoing description is given for clearness of understanding only,and no unnecessary limitations should be understood therefrom, asmodifications within the scope of the invention may be apparent to thosehaving ordinary skill in the art.

The water-soluble films in accordance with the disclosure can be betterunderstood in light of the following example, which is merely intendedto illustrate the water-soluble films and water-soluble packets and arenot meant to limit the scope thereof in any way.

Specific contemplated aspects of the disclosure herein are described inthe following numbered paragraphs.

1. A water-soluble packet, comprising:

-   -   a water-soluble film in the form of a packet and coated by a        powder, the powder comprising a mixture of        -   a powdered lubricant; and        -   an active agent wherein the active agent is not a fragrance.

2. A water-soluble packet, comprising:

-   -   a water-soluble film in the form of a packet and coated by a        powder, the powder comprising        -   a powdered lubricant; and        -   an active agent which comprises a microencapsulated            fragrance.

3. The water-soluble packet of paragraph 1, wherein the active agent ismicroencapsulated.

4. The water-soluble packet according to any one of the precedingparagraphs, wherein the powdered lubricant is selected from the groupconsisting of starches, modified starches, silicas, siloxanes, calciumcarbonate, magnesium carbonate, clay, talc, silicic acid, kaolin,gypsum, zeolites, cylclodextrins, calcium stearate, zinc stearate,alumina, magnesium stearate, alumina, zinc oxide and combinationsthereof.

5. The water-soluble packet according to any one of the precedingparagraphs, wherein the active agent is selected from the groupconsisting of enzymes, oils, flavors, colorants, odor absorbers,fragrances, pesticides, fertilizers, activators, acid catalysts, metalcatalysts, ion scavengers, bleaches, bleach components, fabric softenersor combinations thereof.

6. The water-soluble packet of paragraph 2 or paragraph 3, wherein themicrocapsule is characterized by one or more of the following releasemechanisms: mechanical rupture, dissolution, diffusion, ablation,biodegradation, melt, or a pH triggered release mechanism.

7. The water-soluble packet of any one of the preceding paragraphs,wherein the powdered lubricant is characterized by a mean particle sizein a range of about 1 μm to about 100 μm.

8. The water-soluble packet according to any one of paragraphs 2-5,wherein said microcapsule is selected from one or more of: melamineformaldehyde, polyurethane, urea formaldehyde, chitosan, poly methylmethacrylate, polystyrene, polysulfone, poly tetrahydrofuran, gelatin,gum arabic, starch, polyvinylpyrrolidone, carboxymethylcellulose,hydroxyethylcellulose, methylcellulose, arabinogalactan, polyvinylalcohol, polyacrylic acid, ethylcellulose, polyethylene,polymethacrylate, polyamide, poly (ethylenevinyl acetate), cellulosenitrate, silicones, poly(lactideco-glycolide), paraffin, carnauba,spermaceti, beeswax, stearic acid, stearyl alcohol, glyceryl stearates,shellac, cellulose acetate phthalate, and zein.

9. The water-soluble packet according to any one of the precedingparagraphs, wherein the microcapsule is characterized by a mean particlesize in a range of about 0.1 μm to about 200 μm.

10. The water-soluble packet according to any one of paragraphs 2-15,wherein the mean particle size of the microcapsule is greater than themean particle size of the powdered lubricant, wherein the microcapsuleis selected from one or more of the group consisting of melamineformaldehyde, polyurethane, urea formaldehyde, chitosan, polymethylmethacrylate, polystyrene, polysulfone, poly tetrahydrofuran, gelatin,gum arabic, starch, polyvinyl pyrrolidone, carboxymethylcellulose,hydroxyethylcellulose, methylcellulose, arabinogalactan, polyvinylalcohol, polyacrylic acid, ethylcellulose, polyethylene,polymethacrylate, polyamide, poly (ethylenevinyl acetate), cellulosenitrate, silicones, poly(lactideco-glycolide), paraffin, carnauba,spermaceti, beeswax, stearic acid, stearyl alcohol, glyceryl stearates,shellac, cellulose acetate phthalate, and zein.

11. The water-soluble packet according to any one of paragraphs 2-15,wherein microcapsule agglomerates are formed and the mean microcapsuleagglomerate size is greater than the mean particle size of the powderedlubricant, wherein the microcapsule is selected from one or more of thegroup consisting of melamine formaldehyde, polyurethane, ureaformaldehyde, chitosan, polymethyl methacrylate, polystyrene,polysulfone, polytetrahydrofuran, gelatin, gum arabic, starch, polyvinylpyrrolidone, carboxymethylcellulose, hydroxyethylcellulose,methylcellulose, arabinogalactan, polyvinyl alcohol, polyacrylic acid,ethylcellulose, polyethylene, polymethacrylate, polyamide,poly(ethylenevinyl acetate), cellulose nitrate, silicones,poly(lactidoco-glycolide), paraffin, carnauba, spermaceti, beeswax,stearic acid, stearyl alcohol, glyceryl stearates, shellac, celluloseacetate phthalate, or zein.

12. The water-soluble packet according to any one of the precedingparagraphs, wherein the powder comprises about 1 wt % to about 99 wt %active agent.

13. The water-soluble packet according to any one of the precedingparagraphs, wherein the powder comprises about 1 wt % to about 99 w t%powdered lubricant.

14. The water-soluble packet according to any one of the precedingparagraphs, wherein the powder is present in an amount in a range ofabout 0.01 mg/cm² to about 10 mg/cm².

15. The water-soluble packet according to any one of the precedingparagraphs, wherein the water-soluble film comprises a material selectedfrom the group consisting polyvinyl alcohol, modified polyvinylalcohols, polyacrylates, water-soluble acrylate copolymers,methylcellulose, carboxymethylcellulose, dextrin, ethylcellulose,hydroxyethylcelleulose, hydroxypropyl methylcellulose, malodextrin,polymethacrylates, polyvinyl alcohol copolymers, hydroxypropyl methylcellulose, polyvinyl pyrrolidone, polyalkylene oxides, acrylamide,acrylic acid, and combinations thereof.

16. The water-soluble packet according to any one of the precedingparagraphs, further comprising a solid, liquid, or gel compositionenclosed within the water-soluble film.

17. The water-soluble packet according to paragraph 16, wherein theenclosed composition comprises laundry detergents, bleach and laundryadditives, fabric care, dishwashing, hard surface cleaning, beauty care,skin care, other personal care, or food product compositions.

18. The water-soluble packet according to paragraph 16, wherein theactive agent is capable of a chemical reaction with a component of thecomposition enclosed in the water-soluble film.

19. The water-soluble packet according to paragraph 18, wherein theactive agent is capable of a chemical reaction with a component of thecomposition enclosed in the water-soluble film in an aqueous solution.

20. The water-soluble packet according to paragraph 16, wherein eitherthe active agent is unstable in the presence of a component of thecomposition enclosed within the water-soluble film, or a component ofthe composition enclosed within the water-soluble film is unstable inthe presence of the active agent, or both the active agent and acomponent of the composition enclosed within the water-soluble film areunstable in the presence of each other.

21. The water-soluble packet according to paragraph 19, wherein thecomposition enclosed in the water-soluble film comprises a percarbonate;and the active agent comprises tetraacytylethylenediamine (TAED).

22. A method of providing a water-soluble packet with additionalfunctionality, comprising:

-   -   coating a water-soluble packet with a powder comprising a        powdered lubricant; and    -   an active agent wherein the active agent is not a fragrance.

23. A method of providing a water-soluble packet with additionalfunctionality, comprising:

-   -   coating a water-soluble packet with a powder comprising a        powdered lubricant; and    -   an active agent which comprises a microencapsulated fragrance.

24. The method according to paragraph 22, wherein the active agent ismicroencapsulated.

25. The method according to paragraph 22, 23, or 24, wherein thewater-soluble packet further comprises a solid, liquid, or gelcomposition enclosed within the water-soluble film.

26. The method according to any one of paragraphs 22-24, wherein thepowder coating is present in an amount in a range of about 0.01 mg/cm²to about 10 mg/cm².

27. The method according to any one paragraphs 22-26, wherein thepowdered lubricant is selected from the group consisting of starches,modified starches, silicas, siloxanes, calcium carbonate, magnesiumcarbonate, clay, talc, silicic acid, kaolin, gypsum, zeolites,cyclodextrins, calcium stearate, zinc stearate, magnesium stearate,alumina, zinc oxide and combinations thereof.

28. The method according to any one of paragraphs 22-27, wherein saidactive agent is selected from the group consisting of enzymes, oils,flavors, colorants, odor absorbers, pesticides, fertilizers, activators,acid catalysts, metal catalysts, ion scavengers, bleaches, bleachcomponents, fabric softeners and combinations thereof.

29. The method according to any one of paragraphs 22-28, furthercomprising preparing the coating powder by a process comprising:

-   -   providing a master batch of a first powder comprising a first        powdered lubricant; and    -   mixing the active agent with a portion of the master batch to        form a daughter batch of coating powder.

30. The method according to paragraph 29, wherein a continuous feed ofactive agent is mixed with a continuous feed of the master batch to formthe coating powder.

31. The method according to any one of paragraphs 22-30, wherein theprocess of applying the coating powder to the water-soluble filmcomprises sprinkling, brushing, dusting, or spraying.

32. A water-soluble film coated by a powder, the powder comprising amixture of a powdered lubricant and an active agent, wherein the activeagent is not a fragrance.

33. A water-soluble film coated by a powder, the powder comprising apowdered lubricant and an active agent which comprises amicroencapsulated fragrance.

EXAMPLES Effect of Microencapsulated Fragrances on Pouch Malodor

The effect of a powder coating comprising a starch powdered lubricantand a perfume microcapsule active agent on pouch malodor was evaluated.In this example, malodor was imparted to scent-free pouches to representmalodor that might be produced from a water-soluble film or componentspackaged within water-soluble films during storage. The pouches werecoated with a powder comprising a powdered lubricant (starch) and anactive agent (perfumed microcapsules) and the effect of the perfumemicrocapsules were determined by evaluation by a sensory panel. Fivetypes of pouches were evaluated, including: non-coated, malodor-freepouches (designated “blank”); starch coated, malodor-free pouches(designated “only starch”); starch coated, malodor pouches (designated“malodor+starch”); and pouches treated with malodor and coated with astarch/perfume microcapsules(PMC) powder at two concentrations, 25% ofstarch by weight (designated “malodor+starch+PMC”) and 50% of starch byweight (designated “malodor+starch+PMC 2X”).

The pouches evaluated were 0.6 fl. oz. Triple Action Purex© Ultrapacks(Free and Clear) manufactured by The Dial Corporation (Scottsdale, Az.).Pouches were packaged in stand-up bags (18 pouches/bag) with dimensionsof 185 mm×210 mm. The volume of the bags was 2.2 L without the pouches,headspace in the bag with the pouches was found to be 1.9 L. The “blank”pouches were used as received. Pouches were treated with malodor bydropping into the stand-up bags, cotton balls infused with 200 μm of anaqueous (deionized water) tert-butanethiol (TBT) solution having a TBTconcentration of 300 μl/l. The starch or starch and perfumedmicrocapsule mixture were then added to the pouches.

The starch carrier powder used was a 28 μm foodgrade starch-basedprinting press powder. The “starch only” and the “malodor+starch”pouches were coated with the carrier powder by adding 0.25 g of starchto stand-up bags containing malodor-free pouches and malodor-treatedpouches, respectively. The bags were sealed using zip seal fitments onthe individual bags and were stored overnight.

The perfume microcapsules used were melamine formaldehyde capsules witha perfume oil in the core. The mean diameter of the capsules was 18 μm.The perfume microcapsules were obtained as a slurry in water; the slurrywas spray-dried using a dual fluid melt spray prior to incorporation ofthe microcapsules into the starch carrier powder. The dried perfumemicrocapsules were combined with the starch prior to introduction tostand-up bags containing malodor treated pouches. A measure of 0.0625 gof dried perfume microcapsules was added to 0.25 g of starch and themixture was added to stand-up bags of malodor-treated pouches to formthe “malodor+starch+PMC” pouches. A double measure (0.125 g) of driedperfume microcapsules was added to 0.25 g of starch and the mixtureadded to stand-up bags of malodor-treated pouches to form the“malodor+starch+PMC 2X” pouches. The bags were sealed using zip sealfitments on the individual bags and were stored overnight.

Fourteen panelists were given the sample bags with random numbering andasked to evaluate the odor from the headspace of the bags on a scale ofvery bad to very good (very bad, bad, slightly bad, neutral, slightlygood, good, very good). The responses were given a numerical value from1 (very bad) to 7 (very good).

FIG. 1 shows the interval plot of the numerical value (and 95%confidence interval) of the odor perceived from each pouch type. The“blank” and “only starch” samples were not perceived to be significantlydifferent from each other by the sensory panel. The “Malodor+starch” wasperceived significantly below the no-effect value of 4, with the meanand the 95% confidence interval below 4. All of the pouches treated withthe perfume microcapsule/starch mixture (“malodor+starch+PMC” and“malodor+starch+PMC 2X”) showed positive effects on the panelists withmean values and 95% confidence intervals significantly higher than theno-effect value of 4. The odor perceived at 50% perfume microcapsuleloading was slightly better than the odor perceived at 25% perfumemicrocapsule loading. Thus, the Example demonstrates that thefunctionalized powder is able to overcome malodor.

What is claimed:
 1. A water-soluble packet, comprising: a water-solublefilm in the form of a packet and coated by a powder, the powdercomprising a mixture of a powdered lubricant and an active agent,provided that when the active agent is a fragrance the fragrance ismicroencapsulated.
 2. The water-soluble packet of claim 1, wherein theactive agent is microencapsulated.
 3. The water-soluble packet accordingto claim 1, wherein the powdered lubricant is selected from the groupconsisting of starches, modified starches, silicas, siloxanes, calciumcarbonate, magnesium carbonate, clay, talc, silicic acid, gypsum,zeolites, cylclodextrins, calcium stearate, zinc stearate, alumina,magnesium stearate, alumina, zinc oxide and combinations thereof.
 4. Thewater-soluble packet according to claim 3, wherein the powderedlubricant is kaolin.
 5. The water-soluble packet according to claim 1,wherein the active agent is selected from the group consisting ofenzymes, oils, flavors, colorants, odor absorbers, fragrances,pesticides, fertilizers, activators, acid catalysts, metal catalysts,ion scavengers, bleaches, bleach components, fabric softeners orcombinations thereof.
 6. The water-soluble packet of claim 2, whereinthe microcapsule is characterized by one or more of the followingrelease mechanisms: mechanical rupture, dissolution, diffusion,ablation, biodegradation, melt, or a pH triggered release mechanism. 7.The water-soluble packet of claim 1, wherein the powdered lubricant ischaracterized by a mean particle size in a range of about 1 μm to about100 μm.
 8. The water-soluble packet according to claim 2, wherein saidmicrocapsule is selected from one or more of: melamine formaldehyde,polyurethane, urea formaldehyde, chitosan, poly methyl methacrylate,polystyrene, polysulfone, poly tetrahydrofuran, gelatin, gum arabic,starch, polyvinylpyrrolidone, carboxymethylcellulose,hydroxyethylcellulose, methylcellulose, arabinogalactan, polyvinylalcohol, polyacrylic acid, ethylcellulose, polyethylene,polymethacrylate, polyamide, poly (ethylenevinyl acetate), cellulosenitrate, silicones, poly(lactideco-glycolide), paraffin, carnauba,spermaceti, beeswax, stearic acid, stearyl alcohol, glyceryl stearates,shellac, cellulose acetate phthalate, and zein.
 9. The water-solublepacket according to claim 2, wherein the microcapsule is characterizedby a mean particle size in a range of about 0.1 μm to about 200 μm. 10.The water-soluble packet according to claim 2, wherein the mean particlesize of the microcapsule is greater than the mean particle size of thepowdered lubricant, wherein the microcapsule is selected from one ormore of the group consisting of melamine formaldehyde, polyurethane,urea formaldehyde, chitosan, polymethyl methacrylate, polystyrene,polysulfone, poly tetrahydrofuran, gelatin, gum arabic, starch,polyvinyl pyrrolidone, carboxymethylcellulose, hydroxyethylcellulose,methylcellulose, arabinogalactan, polyvinyl alcohol, polyacrylic acid,ethylcellulose, polyethylene, polymethacrylate, polyamide, poly(ethylenevinyl acetate), cellulose nitrate, silicones,poly(lactideco-glycolide), paraffin, carnauba, spermaceti, beeswax,stearic acid, stearyl alcohol, glyceryl stearates, shellac, celluloseacetate phthalate, and zein.
 11. The water-soluble packet according toclaim 2, wherein microcapsule agglomerates are formed and the meanmicrocapsule agglomerate size is greater than the mean particle size ofthe powdered lubricant, wherein the microcapsule is selected from one ormore of the group consisting of melamine formaldehyde, polyurethane,urea formaldehyde, chitosan, polymethyl methacrylate, polystyrene,polysulfone, polytetrahydrofuran, gelatin, gum arabic, starch, polyvinylpyrrolidone, carboxymethylcellulose, hydroxyethylcellulose,methylcellulose, arabinogalactan, polyvinyl alcohol, polyacrylic acid,ethylcellulose, polyethylene, polymethacrylate, polyamide,poly(ethylenevinyl acetate), cellulose nitrate, silicones,poly(lactidoco-glycolide), paraffin, carnauba, spermaceti, beeswax,stearic acid, stearyl alcohol, glyceryl stearates, shellac, celluloseacetate phthalate, or zein.
 12. The water-soluble packet according toclaim 1, wherein the powder comprises about 1 wt % to about-99 wt %active agent.
 13. The water-soluble packet according to claim 1, whereinthe powder comprises about 1 wt % to about-99 wt % powdered lubricant.14. The water-soluble packet according to claim 1, wherein the powder ispresent in an amount in a range of about 0.01 mg/cm² to about 10 mg/cm².15. The water-soluble packet according to claim 1, wherein thewater-soluble film comprises a material selected from the groupconsisting polyvinyl alcohol, modified polyvinyl alcohols,polyacrylates, water-soluble acrylate copolymers, methylcellulose,carboxymethylcellulose, dextrin, ethylcellulose, hydroxyethylcelleulose,hydroxypropyl methylcellulose, malodextrin, polymethacrylates, polyvinylalcohol copolymers, hydroxypropyl methyl cellulose, polyvinylpyrrolidone, polyalkylene oxides, acrylamide, acrylic acid, andcombinations thereof.
 16. The water-soluble packet according to claim 1,further comprising a solid, liquid, or gel composition enclosed withinthe water-soluble packet.
 17. The water-soluble packet according toclaim 16, wherein the enclosed composition comprises laundry detergents,bleach and laundry additives, fabric care, dishwashing, hard surfacecleaning, beauty care, skin care, other personal care, or food productcompositions.
 18. The water-soluble packet according to claim 16,wherein the active agent is capable of a chemical reaction with acomponent of the composition enclosed in the water-soluble film.
 19. Thewater-soluble packet according to claim 18, wherein the active agent iscapable of a chemical reaction with a component of the compositionenclosed in the water-soluble film in an aqueous solution.
 20. Thewater-soluble packet according to claim 16, wherein either the activeagent is unstable in the presence of a component of the compositionenclosed within the water-soluble film, or a component of thecomposition enclosed within the water-soluble film is unstable in thepresence of the active agent, or both the active agent and a componentof the composition enclosed within the water-soluble film are unstablein the presence of each other.
 21. The water-soluble packet according toclaim 19, wherein the composition enclosed in the water-soluble filmcomprises a percarbonate; and the active agent comprisestetraacytylethylenediamine (TAED).
 22. A method of providing awater-soluble packet with additional functionality, comprising: coatinga water-soluble film in the form of a water-soluble packet with a powdercomprising a powdered lubricant and an active agent, provided that whenthe active agent is a fragrance the fragrance is microencapsulated. 23.A water-soluble film coated by a powder, the powder comprising a mixtureof a powdered lubricant and an active agent, provided that when theactive agent is a fragrance the fragrance is microencapsulated.